3hbl

From Proteopedia

(Difference between revisions)

Revision as of 11:50, 25 December 2014

Crystal Structure of S. aureus Pyruvate Carboxylase T908A Mutant

Structural highlights

3hbl 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:	, ,
Related:	3hb9
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/3hbl"

@@ Line 8: / Line 8: @@
 <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=3hbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hbl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hbl RCSB], [http://www.ebi.ac.uk/pdbsum/3hbl 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]]

3hbl

From Proteopedia

Revision as of 11:50, 25 December 2014

Crystal Structure of S. aureus Pyruvate Carboxylase T908A Mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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