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{{Short description|Family of transport proteins}}
{{Pfam box {{Pfam box
| Symbol = A3P053 | Symbol = A3P053
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==Structure and function== ==Structure and function==
Known proteins in the AGCS family are between 445 and 550 amino acyl residues in length and possess 8 to 12 putative transmembrane α-helical spanners. Members may possess 11 transmembrane segments (TMSs), as seems to be true for DagA () and AgcS (), although Acp () has only 8 TMSs, perhaps the result of truncation. As of early 2016, there does not appear to be any 3D crystal structure data available for these proteins. Members of the AGCS family have been found in bacteria and archaea, such as extremophile halotolerant cyanobacterium ''Aphanothece halophytica,'' and thermophilic bacteria, ''Bacillus'' ''PS3''.<ref name="Bualuang">{{cite journal | vauthors = Bualuang A, Kageyama H, Tanaka Y, Incharoensakdi A, Takabe T | title = Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica | journal = Bioscience, Biotechnology, and Biochemistry | volume = 79 | issue = 2 | pages = 230–5 | date = 2015 | pmid = 25421789 | doi = 10.1080/09168451.2014.968091 | s2cid = 205616830 }}</ref><ref>{{cite journal | vauthors = Kanamori M, Kamata H, Yagisawa H, Hirata H | title = Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli | journal = Journal of Biochemistry | volume = 125 | issue = 3 | pages = 454–9 | date = March 1999 | pmid = 10050032 | doi = 10.1093/oxfordjournals.jbchem.a022308 }}</ref> As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family ().<ref name=TCDB/> High-resolution structures of AgcS from ''Methanococcus maripaludis'' were obtained using X-ray crystallography and released in 2019 and show structural homology to other members of the ] superfamily of transporters<ref>{{Cite journal|last=Ma|first=Jinming|last2=Lei|first2=Hsiang-Ting|last3=Reyes|first3=Francis E.|last4=Sanchez-Martinez|first4=Silvia|last5=Sarhan|first5=Maen F.|last6=Hattne|first6=Johan|last7=Gonen|first7=Tamir|date=2019-02-05|title=Structural basis for substrate binding and specificity of a sodium–alanine symporter AgcS|url=https://www.pnas.org/content/116/6/2086|journal=Proceedings of the National Academy of Sciences|language=en|volume=116|issue=6|pages=2086–2090|doi=10.1073/pnas.1806206116|issn=0027-8424|pmc=6369739|pmid=30659158}}</ref>. Known proteins in the AGCS family are between 445 and 550 amino acyl residues in length and possess 8 to 12 putative transmembrane α-helical spanners. Members may possess 11 transmembrane segments (TMSs), as seems to be true for DagA () and AgcS (), although Acp () has only 8 TMSs, perhaps the result of truncation. As of early 2016, there does not appear to be any 3D crystal structure data available for these proteins. Members of the AGCS family have been found in bacteria and archaea, such as extremophile halotolerant cyanobacterium ''Aphanothece halophytica,'' and thermophilic bacteria, ''Bacillus'' ''PS3''.<ref name="Bualuang">{{cite journal | vauthors = Bualuang A, Kageyama H, Tanaka Y, Incharoensakdi A, Takabe T | title = Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica | journal = Bioscience, Biotechnology, and Biochemistry | volume = 79 | issue = 2 | pages = 230–5 | date = 2015 | pmid = 25421789 | doi = 10.1080/09168451.2014.968091 | s2cid = 205616830 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Kanamori M, Kamata H, Yagisawa H, Hirata H | title = Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli | journal = Journal of Biochemistry | volume = 125 | issue = 3 | pages = 454–9 | date = March 1999 | pmid = 10050032 | doi = 10.1093/oxfordjournals.jbchem.a022308 }}</ref> As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family ().<ref name=TCDB/> High-resolution structures of AgcS from ''Methanococcus maripaludis'' were obtained using X-ray crystallography and released in 2019 and show structural homology to other members of the ] superfamily of transporters.<ref>{{cite journal | vauthors = Ma J, Lei HT, Reyes FE, Sanchez-Martinez S, Sarhan MF, Hattne J, Gonen T | title = Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 116 | issue = 6 | pages = 2086–2090 | date = February 2019 | pmid = 30659158 | pmc = 6369739 | doi = 10.1073/pnas.1806206116 | bibcode = 2019PNAS..116.2086M | doi-access = free }}</ref>


===Transport reaction=== ===Transport reaction===
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== Further reading == == Further reading ==
{{refbegin}} {{refbegin}}
* {{cite journal | vauthors = Rodionov DA, Hebbeln P, Eudes A, ter Beek J, Rodionova IA, Erkens GB, Slotboom DJ, Gelfand MS, Osterman AL, Hanson AD, Eitinger T | title = A novel class of modular transporters for vitamins in prokaryotes | journal = Journal of Bacteriology | volume = 191 | issue = 1 | pages = 42–51 | date = January 2009 | pmid = 18931129 | pmc = 2612444 | doi = 10.1128/JB.01208-08 }} * {{cite journal | vauthors = Rodionov DA, Hebbeln P, Eudes A, ter Beek J, Rodionova IA, Erkens GB, Slotboom DJ, Gelfand MS, Osterman AL, Hanson AD, Eitinger T | display-authors = 6 | title = A novel class of modular transporters for vitamins in prokaryotes | journal = Journal of Bacteriology | volume = 191 | issue = 1 | pages = 42–51 | date = January 2009 | pmid = 18931129 | pmc = 2612444 | doi = 10.1128/JB.01208-08 }}
* {{cite journal | vauthors = Kamata H, Akiyama S, Morosawa H, Ohta T, Hamamoto T, Kambe T, Kagawa Y, Hirata H | title = Primary structure of the alanine carrier protein of thermophilic bacterium PS3 | journal = The Journal of Biological Chemistry | volume = 267 | issue = 30 | pages = 21650–5 | date = October 1992 | pmid = 1400476 }} * {{cite journal | vauthors = Kamata H, Akiyama S, Morosawa H, Ohta T, Hamamoto T, Kambe T, Kagawa Y, Hirata H | display-authors = 6 | title = Primary structure of the alanine carrier protein of thermophilic bacterium PS3 | journal = The Journal of Biological Chemistry | volume = 267 | issue = 30 | pages = 21650–5 | date = October 1992 | doi = 10.1016/S0021-9258(19)36661-X | pmid = 1400476 | doi-access = free }}
{{refend}} {{refend}}


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{{membrane-protein-stub}} {{membrane-protein-stub}}

Latest revision as of 04:26, 29 November 2023

Family of transport proteins Protein family
Alanine/glycine:cation symporter (AGCS) family protein
Identifiers
SymbolA3P053
PfamPF01235
InterProIPR001463
PROSITEPS00873
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Members of the Alanine or Glycine:Cation Symporter (AGCS) Family (TC# 2.A.25) transport alanine and/or glycine in symport with Na and or H.

Structure and function

Known proteins in the AGCS family are between 445 and 550 amino acyl residues in length and possess 8 to 12 putative transmembrane α-helical spanners. Members may possess 11 transmembrane segments (TMSs), as seems to be true for DagA (TC# 2.A.25.1.1) and AgcS (TC# 2.A.25.1.3), although Acp (TC# 2.A.25.1.2) has only 8 TMSs, perhaps the result of truncation. As of early 2016, there does not appear to be any 3D crystal structure data available for these proteins. Members of the AGCS family have been found in bacteria and archaea, such as extremophile halotolerant cyanobacterium Aphanothece halophytica, and thermophilic bacteria, Bacillus PS3. As of 2015, only three members of the family have been functionally characterized. These proteins show limited sequence similarity in the APC family (TC# 2.A.3). High-resolution structures of AgcS from Methanococcus maripaludis were obtained using X-ray crystallography and released in 2019 and show structural homology to other members of the Amino acid-Polyamine-Organocation superfamily of transporters.

Transport reaction

The generalized transport reaction catalyzed by the AGCS family is:

alanine or glycine (out) + Na or H (out) → alanine or glycine (in) + Na or H (in).

Proteins in the AGCS family

There are currently 10 proteins belonging to the AGCS family. These proteins and their descriptions can be found in the Transporter Classification Database.

References

  1. Bualuang A, Kageyama H, Tanaka Y, Incharoensakdi A, Takabe T (2015). "Functional characterization of a member of alanine or glycine: cation symporter family in halotolerant cyanobacterium Aphanothece halophytica". Bioscience, Biotechnology, and Biochemistry. 79 (2): 230–5. doi:10.1080/09168451.2014.968091. PMID 25421789. S2CID 205616830.
  2. Kanamori M, Kamata H, Yagisawa H, Hirata H (March 1999). "Overexpression of the alanine carrier protein gene from thermophilic bacterium PS3 in Escherichia coli". Journal of Biochemistry. 125 (3): 454–9. doi:10.1093/oxfordjournals.jbchem.a022308. PMID 10050032.
  3. ^ Saier MH. "2.A.25 The Alanine or Glycine:Cation Symporter (AGCS) Family". Transporter Classification Database. Saier Lab Bioinformatics Group / SDSC.
  4. Ma J, Lei HT, Reyes FE, Sanchez-Martinez S, Sarhan MF, Hattne J, Gonen T (February 2019). "Structural basis for substrate binding and specificity of a sodium-alanine symporter AgcS". Proceedings of the National Academy of Sciences of the United States of America. 116 (6): 2086–2090. Bibcode:2019PNAS..116.2086M. doi:10.1073/pnas.1806206116. PMC 6369739. PMID 30659158.

Further reading

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