1o8u

From Proteopedia

(Difference between revisions)

Current revision

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Structural highlights

1o8u is a 6 chain structure with sequence from Rhodococcus erythropolis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAMK_RHOSO Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.^[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

6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily that catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572). The native structure of OCH has been solved at 2.0-A resolution with selenomethionine multiple wave anomalous dispersion and refined to a final R(free) of 19.0. The structure of OCH consists of a dimer of trimers that resembles the "parent" enzyme of the superfamily, enoyl-CoA hydratase. In contrast to enoyl-CoA hydratase, however, two octahedrally coordinated sodium atoms are found at the 3-fold axis of the hexamer of OCH, and the C-terminal helix of OCH does not form a discrete domain. Models of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.

The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.,Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. PMID:12421807^[3]

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

References

↑ Grogan G, Roberts GA, Bougioukou D, Turner NJ, Flitsch SL. The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily. J Biol Chem. 2001 Apr 20;276(16):12565-72. PMID:11278926 doi:10.1074/jbc.M011538200
↑ Leonard PM, Grogan G. Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog. J Biol Chem. 2004 Jul 23;279(30):31312-7. Epub 2004 May 11. PMID:15138275 doi:10.1074/jbc.M403514200
↑ Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G. The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily. J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. PMID:12421807 doi:10.1074/jbc.M211188200

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/1o8u"

@@ Line 3: / Line 3: @@
 <StructureSection load='1o8u' size='340' side='right'caption='[[1o8u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1o8u]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O8U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1o8u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8u OCA], [http://pdbe.org/1o8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o8u RCSB], [http://www.ebi.ac.uk/pdbsum/1o8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8u ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=1o8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8u OCA], [https://pdbe.org/1o8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o8u RCSB], [https://www.ebi.ac.uk/pdbsum/1o8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8u ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAMK_RHOSO CAMK_RHOSO] Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.<ref>PMID:11278926</ref> <ref>PMID:15138275</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 30: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Mycobacterium erythropolis gray and thornton 1928]]
 [[Category: Large Structures]]
-[[Category: Grogan, G]]
+[[Category: Rhodococcus erythropolis]]
-[[Category: Turkenburg, J P]]
+[[Category: Grogan G]]
-[[Category: Verma, C S]]
+[[Category: Turkenburg JP]]
-[[Category: Walsh, M A]]
+[[Category: Verma CS]]
-[[Category: Whittingham, J L]]
+[[Category: Walsh MA]]
-[[Category: Crotonase]]
+[[Category: Whittingham JL]]
-[[Category: Hydrolase]]
-[[Category: Rhodococcuse]]
-[[Category: Terpene metabolism]]

1o8u

From Proteopedia

Current revision

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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