3ho8

From Proteopedia

(Difference between revisions)

Revision as of 20:00, 25 December 2014

Crystal Structure of S. aureus Pyruvate Carboxylase in complex with Coenzyme A

Structural highlights

3ho8 is a 4 chain structure with sequence from Staphylococcus aureus subsp. aureus mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	pycA, Pyruvate Carboxylase, SAV1114 (Staphylococcus aureus subsp. aureus Mu50)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q99UY8_STAAM] Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (By similarity).[PIRNR:PIRNR001594]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Pyruvate carboxylase (PC) is a conserved metabolic enzyme with important cellular functions. We report crystallographic and cryo-electron microscopy (EM) studies of Staphylococcus aureus PC (SaPC) in complex with acetyl-CoA, an allosteric activator, and mutagenesis, biochemical, and structural studies of the biotin binding site of its carboxyltransferase (CT) domain. The disease-causing A610T mutation abolishes catalytic activity by blocking biotin binding to the CT active site, and Thr908 might play a catalytic role in the CT reaction. The crystal structure of SaPC in complex with CoA reveals a symmetrical tetramer, with one CoA molecule bound to each monomer, and cryo-EM studies confirm the symmetrical nature of the tetramer. These observations are in sharp contrast to the highly asymmetrical tetramer of Rhizobium etli PC in complex with ethyl-CoA. Our structural information suggests that acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of PC that might be catalytically more competent.

A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A.,Yu LP, Xiang S, Lasso G, Gil D, Valle M, Tong L Structure. 2009 Jun 10;17(6):823-32. PMID:19523900^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yu LP, Xiang S, Lasso G, Gil D, Valle M, Tong L. A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A. Structure. 2009 Jun 10;17(6):823-32. PMID:19523900 doi:10.1016/j.str.2009.04.008

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ho8"

@@ Line 7: / Line 7: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ho8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ho8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ho8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ho8 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q99UY8_STAAM Q99UY8_STAAM]] Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second (By similarity).[PIRNR:PIRNR001594]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3ho8

From Proteopedia

Revision as of 20:00, 25 December 2014

Crystal Structure of S. aureus Pyruvate Carboxylase in complex with Coenzyme A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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