2ahu: Difference between revisions
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==Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.== | |||
<StructureSection load='2ahu' size='340' side='right'caption='[[2ahu]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ahu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2AHU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahu OCA], [https://pdbe.org/2ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahu RCSB], [https://www.ebi.ac.uk/pdbsum/2ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahu ProSAT]</span></td></tr> | |||
</table> | |||
| | == Function == | ||
[https://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]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ah/2ahu_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2ahu ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:16253988</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ahu" style="background-color:#fffaf0;"></div> | |||
[[Category: Escherichia coli]] | == References == | ||
[[Category: | <references/> | ||
[[Category: Ajamian | __TOC__ | ||
</StructureSection> | |||
[[Category: Cygler | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Fraser | [[Category: Large Structures]] | ||
[[Category: Iannuzzi | [[Category: Ajamian E]] | ||
[[Category: Kernaghan | [[Category: Cygler M]] | ||
[[Category: Li | [[Category: Fraser ME]] | ||
[[Category: Matte | [[Category: Iannuzzi P]] | ||
[[Category: Rangarajan | [[Category: Kernaghan SD]] | ||
[[Category: Li Y]] | |||
[[Category: Matte A]] | |||
[[Category: Rangarajan ES]] | |||
