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2ahv

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Revision as of 06:57, 9 May 2018

Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1

Structural highlights

2ahv 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.
Ligands:
Related:	2ahu, 2ahw
Gene:	YdiF (ECO57)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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/2ahv"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1==
 <StructureSection load='2ahv' size='340' side='right' caption='[[2ahv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahu|2ahu]], [[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=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=2ahv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahv OCA], [http://pdbe.org/2ahv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahv RCSB], [http://www.ebi.ac.uk/pdbsum/2ahv 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=2ahv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahv OCA], [http://pdbe.org/2ahv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahv RCSB], [http://www.ebi.ac.uk/pdbsum/2ahv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahv ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/2ahv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/2ahv_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ahv ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2ahv

From Proteopedia

Revision as of 06:57, 9 May 2018

Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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