2vep

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:58, 9 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2vep.png|left|200px]]
 
-
{{STRUCTURE_2vep| PDB=2vep | SCENE= }}
+
==Crystal Structure Of The Full Length Bifunctional Enzyme Pria==
 +
<StructureSection load='2vep' size='340' side='right'caption='[[2vep]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2vep]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VEP 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]] 1.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2vep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vep OCA], [https://pdbe.org/2vep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vep RCSB], [https://www.ebi.ac.uk/pdbsum/2vep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vep ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HIS4_STRCO HIS4_STRCO] Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan.[HAMAP-Rule:MF_01014]
 +
== 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/ve/2vep_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=2vep ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Two structures of phosphoribosyl isomerase A (PriA) from Streptomyces coelicolor, involved in both histidine and tryptophan biosynthesis, were solved at 1.8A resolution. A closed conformer was obtained, which represents the first complete structure of PriA, revealing hitherto unnoticed molecular interactions and the occurrence of conformational changes. Inspection of these conformers, including ligand-docking simulations, allowed identification of residues involved in substrate recognition, chemical catalysis and conformational changes. These predictions were validated by mutagenesis and functional analysis. Arg19 and Ser81 were shown to play critical roles within the carboxyl and amino phosphate-binding sites, respectively; the catalytic residues Asp11 and Asp130 are responsible for both activities; and Thr166 and Asp171, which make an unusual contact, are likely to elicit the conformational changes needed for adopting the active site architectures. This represents the first report of the structure/function relationship of this (betaalpha)8-isomerase.
-
===CRYSTAL STRUCTURE OF THE FULL LENGTH BIFUNCTIONAL ENZYME PRIA===
+
The structure/function relationship of a dual-substrate (betaalpha)8-isomerase.,Wright H, Noda-Garcia L, Ochoa-Leyva A, Hodgson DA, Fulop V, Barona-Gomez F Biochem Biophys Res Commun. 2008 Jan 4;365(1):16-21. Epub 2007 Oct 29. PMID:17967415<ref>PMID:17967415</ref>
-
{{ABSTRACT_PUBMED_17967415}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2vep" style="background-color:#fffaf0;"></div>
-
[[2vep]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEP OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:017967415</ref><references group="xtra"/>
+
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
-
[[Category: Barona-Gomez, F.]]
+
[[Category: Barona-Gomez F]]
-
[[Category: Fulop, V.]]
+
[[Category: Fulop V]]
-
[[Category: Hodgson, D A.]]
+
[[Category: Hodgson DA]]
-
[[Category: Noda-Garcia, L.]]
+
[[Category: Noda-Garcia L]]
-
[[Category: Ochoa-Leyva, A.]]
+
[[Category: Ochoa-Leyva A]]
-
[[Category: Wright, H.]]
+
[[Category: Wright H]]
-
[[Category: Amino-acid biosynthesis]]
+
-
[[Category: Aromatic amino acid biosynthesis]]
+
-
[[Category: Evolution of substrate specificity]]
+
-
[[Category: Histidine biosynthesis]]
+
-
[[Category: Isomerase]]
+
-
[[Category: Pria]]
+
-
[[Category: Tryptophan biosynthesis]]
+

Current revision

Crystal Structure Of The Full Length Bifunctional Enzyme Pria

PDB ID 2vep

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vep"
Personal tools