2imd

From Proteopedia

(Difference between revisions)

Revision as of 09:36, 11 September 2015

Structure of SeMet 2-hydroxychromene-2-carboxylate isomerase (HCCA isomerase)

Structural highlights

2imd is a 1 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
NonStd Res:
Related:	1r4w, 2ime, 2imf
Gene:	nahD ("Bacillus fluorescens putidus" Flugge 1886)
Activity:	Glutathione transferase, with EC number 2.5.1.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[NAHD_PSEPU] Involved in the naphthalene catabolic pathway. Catalyzes the reversible glutathione-dependent isomerization of 2-hydroxychromene-2-carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA).^[1] ^[2]

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

The enzyme 2-hydroxychromene-2-carboxylic acid (HCCA) isomerase catalyzes the glutathione (GSH)-dependent interconversion (Keq = 1.5) of HCCA and trans-o-hydroxybenzylidene pyruvic acid (tHBPA) in the naphthalene catabolic pathway of Pseudomonas putida. The dimeric protein binds one molecule of GSH very tightly (Kd approximately 5 nM) and a second molecule of GSH with much lower affinity (Kd approximately 2 to 11 microM). The enzyme is unstable in the absence of GSH. The turnover number in the forward direction (47 s(-1) at 25 degrees C) greatly exceeds off rates for GSH (koff approximately 10(-3) to 10(-2) s(-1) at 10 degrees C), suggesting that GSH acts as a tightly bound cofactor in the reaction. The crystal structure of the enzyme at 1.7 A resolution reveals that the isomerase is closely related to class kappa GSH transferases. Diffraction quality crystals could only be obtained in the presence of GSH and HCCA/tHBPA. Clear electron density is seen for GSH. Electron density for the organic substrates is located near the GSH and is best modeled to include both HCCA and tHBPA at occupancies of 0.5 for each. Although there is no electron density connecting the sulfur of GSH to the organic substrates, the sulfur is located very close (2.78 A) to C7 of HCCA. Taken together, the results suggest that the isomerization reaction involves a short-lived covalent adduct between the sulfur of GSH and C7 of the substrate.

2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida.,Thompson LC, Ladner JE, Codreanu SG, Harp J, Gilliland GL, Armstrong RN Biochemistry. 2007 Jun 12;46(23):6710-22. Epub 2007 May 18. PMID:17508726^[3]

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

References

↑ Eaton RW. Organization and evolution of naphthalene catabolic pathways: sequence of the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid. J Bacteriol. 1994 Dec;176(24):7757-62. PMID:8002605
↑ Eaton RW, Chapman PJ. Bacterial metabolism of naphthalene: construction and use of recombinant bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent reactions. J Bacteriol. 1992 Dec;174(23):7542-54. PMID:1447127
↑ Thompson LC, Ladner JE, Codreanu SG, Harp J, Gilliland GL, Armstrong RN. 2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry. 2007 Jun 12;46(23):6710-22. Epub 2007 May 18. PMID:17508726 doi:10.1021/bi700356u

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/2imd"

@@ Line 2: / Line 2: @@
 <StructureSection load='2imd' size='340' side='right' caption='[[2imd]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2imd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IMD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2imd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IMD FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2C2:(2S)-2-HYDROXY-2H-CHROMENE-2-CARBOXYLIC+ACID'>2C2</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TOH:(3E)-4-(2-HYDROXYPHENYL)-2-OXOBUT-3-ENOIC+ACID'>TOH</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r4w|1r4w]], [[2ime|2ime]], [[2imf|2imf]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nahD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 Pseudomonas putida])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nahD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </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=2imd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2imd RCSB], [http://www.ebi.ac.uk/pdbsum/2imd 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=2imd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2imd OCA], [http://pdbe.org/2imd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2imd RCSB], [http://www.ebi.ac.uk/pdbsum/2imd PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2imd" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Bacillus fluorescens putidus flugge 1886]]
 [[Category: Glutathione transferase]]
-[[Category: Pseudomonas putida]]
 [[Category: Armstrong, R N]]
 [[Category: Codreanu, S G]]

2imd

From Proteopedia

Revision as of 09:36, 11 September 2015

Structure of SeMet 2-hydroxychromene-2-carboxylate isomerase (HCCA isomerase)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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