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1otf

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Revision as of 23:27, 11 September 2015

4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM

Structural highlights

1otf is a 6 chain structure with sequence from Pseuf. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	DMPL (PSEUF)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[4OT_PSEUF] Catalyzes the ketonization of 2-hydroxymuconate stereoselectively to yield 2-oxo-3-hexenedioate.

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

5-Carboxymethyl-2-hydroxymuconate isomerase (CHMI) and 4-oxalocrotonate tautomerase (4-OT) are enzymes that catalyze the isomerization of unsaturated ketones. They share a common enzyme mechanism, although they show a preference for different substrates. There is no apparent sequence homology between the enzymes. To investigate the molecular mechanism and the basis for their substrate specificity, we have determined the crystal structures of the two enzymes at high resolution. 4-OT is hexameric, with the subunits arranged with 32 symmetry. CHMI is trimeric and has extensive contacts between subunits, which include secondary structural elements. The central core of the CHMI monomer has a fold similar to a 4-OT dimer, but the secondary structural elements that form the subunit contacts around the 3-fold axis are different in the two enzymes. The region of greatest similarity between the two enzymes is a large pocket that is proposed to be the active site. The enzymes appear to operate via a "one-base" mechanism, and the possible role of residues in this pocket is discussed in view of this idea. Finally, the molecular basis for substrate specificity in the two enzymes is discussed.

Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases.,Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB Biochemistry. 1996 Jan 23;35(3):792-802. PMID:8547259^[1]

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

References

↑ Subramanya HS, Roper DI, Dauter Z, Dodson EJ, Davies GJ, Wilson KS, Wigley DB. Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. Biochemistry. 1996 Jan 23;35(3):792-802. PMID:8547259 doi:http://dx.doi.org/10.1021/bi951732k

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/1otf"

@@ Line 2: / Line 2: @@
 <StructureSection load='1otf' size='340' side='right' caption='[[1otf]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1otf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OTF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1otf]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseuf Pseuf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OTF FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DMPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DMPL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=79676 PSEUF])</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=1otf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1otf RCSB], [http://www.ebi.ac.uk/pdbsum/1otf 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=1otf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1otf OCA], [http://pdbe.org/1otf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1otf RCSB], [http://www.ebi.ac.uk/pdbsum/1otf PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1otf" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Pseudomonas sp]]
+[[Category: Pseuf]]
 [[Category: Dauter, Z]]
 [[Category: Davies, G J]]

1otf

From Proteopedia

Revision as of 23:27, 11 September 2015

4-OXALOCROTONATE TAUTOMERASE-TRICLINIC CRYSTAL FORM

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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