2ahu

From Proteopedia

(Difference between revisions)

Revision as of 08:30, 11 September 2015

Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.

Structural highlights

2ahu is a 4 chain structure with sequence from Eco57. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	2ahv, 2ahw
Gene:	YdiF (ECO57)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[YDIF_ECO57] CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.^[1]

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

Coenzyme A transferases are involved in a broad range of biochemical processes in both prokaryotes and eukaryotes, and exhibit a diverse range of substrate specificities. The YdiF protein from Escherichia coli O157:H7 is an acyl-CoA transferase of unknown physiological function, and belongs to a large sequence family of CoA transferases, present in bacteria to humans, which utilize oxoacids as acceptors. In vitro measurements showed that YdiF displays enzymatic activity with short-chain acyl-CoAs. The crystal structures of YdiF and its complex with CoA, the first co-crystal structure for any Family I CoA transferase, have been determined and refined at 1.9 and 2.0 A resolution, respectively. YdiF is organized into tetramers, with each monomer having an open alpha/beta structure characteristic of Family I CoA transferases. Co-crystallization of YdiF with a variety of CoA thioesters in the absence of acceptor carboxylic acid resulted in trapping a covalent gamma-glutamyl-CoA thioester intermediate. The CoA binds within a well defined pocket at the N- and C-terminal domain interface, but makes contact only with the C-terminal domain. The structure of the YdiF complex provides a basis for understanding the different catalytic steps in the reaction of Family I CoA transferases.

Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.,Rangarajan ES, Li Y, Ajamian E, Iannuzzi P, Kernaghan SD, Fraser ME, Cygler M, Matte A J Biol Chem. 2005 Dec 30;280(52):42919-28. Epub 2005 Oct 27. PMID:16253988^[2]

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

References

↑ Rangarajan ES, Li Y, Ajamian E, Iannuzzi P, Kernaghan SD, Fraser ME, Cygler M, Matte A. Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases. J Biol Chem. 2005 Dec 30;280(52):42919-28. Epub 2005 Oct 27. PMID:16253988 doi:10.1074/jbc.M510522200
↑ Rangarajan ES, Li Y, Ajamian E, Iannuzzi P, Kernaghan SD, Fraser ME, Cygler M, Matte A. Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases. J Biol Chem. 2005 Dec 30;280(52):42919-28. Epub 2005 Oct 27. PMID:16253988 doi:10.1074/jbc.M510522200

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/2ahu"

@@ Line 2: / Line 2: @@
 <StructureSection load='2ahu' size='340' side='right' caption='[[2ahu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ahu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ahu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHU FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahv|2ahv]], [[2ahw|2ahw]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YdiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YdiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
-<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=2ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ahu RCSB], [http://www.ebi.ac.uk/pdbsum/2ahu PDBsum]</span></td></tr>
+<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=2ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahu OCA], [http://pdbe.org/2ahu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahu RCSB], [http://www.ebi.ac.uk/pdbsum/2ahu PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q8X5X6_ECO57 Q8X5X6_ECO57]] CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.
+[[http://www.uniprot.org/uniprot/YDIF_ECO57 YDIF_ECO57]] CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.<ref>PMID:16253988</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ahu" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Eco57]]
 [[Category: Ajamian, E]]
 [[Category: Structural genomic]]

2ahu

From Proteopedia

Revision as of 08:30, 11 September 2015

Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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