This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2ahv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:24, 23 August 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2ahv.png|left|200px]]
 
-
<!--
+
==Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1==
-
The line below this paragraph, containing "STRUCTURE_2ahv", creates the "Structure Box" on the page.
+
<StructureSection load='2ahv' size='340' side='right'caption='[[2ahv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2ahv]] 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=2AHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHV FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
-
{{STRUCTURE_2ahv| PDB=2ahv | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ahv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahv OCA], [https://pdbe.org/2ahv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahv RCSB], [https://www.ebi.ac.uk/pdbsum/2ahv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahv 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/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/main_output.php?pdb_ID=2ahv 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.
-
===Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1===
+
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_16253988}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 2ahv" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 16253988 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16253988}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Escherichia coli O157:H7]]
-
2AHV is a 4 chains structure of sequences from [http://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=2AHV OCA].
+
[[Category: Large Structures]]
-
 
+
[[Category: Ajamian E]]
-
==Reference==
+
[[Category: Cygler M]]
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/16253988 16253988]
+
[[Category: Fraser ME]]
-
[[Category: Escherichia coli o157:h7]]
+
[[Category: Iannuzzi P]]
-
[[Category: Ajamian, E.]]
+
[[Category: Kernaghan SD]]
-
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
+
[[Category: Li Y]]
-
[[Category: Cygler, M.]]
+
[[Category: Matte A]]
-
[[Category: Fraser, M E.]]
+
[[Category: Rangarajan ES]]
-
[[Category: Iannuzzi, P.]]
+
-
[[Category: Kernaghan, S D.]]
+
-
[[Category: Li, Y.]]
+
-
[[Category: Matte, A.]]
+
-
[[Category: Rangarajan, E S.]]
+
-
[[Category: Bsgi]]
+
-
[[Category: Coa transferase]]
+
-
[[Category: Glutamyl thioester]]
+
-
[[Category: Montreal-kingston bacterial structural genomics initiative]]
+
-
[[Category: Structural genomic]]
+
-
[[Category: Ydif]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 15:13:29 2008''
+

Current revision

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

PDB ID 2ahv

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools