3hzz: Difference between revisions

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<StructureSection load='3hzz' size='340' side='right'caption='[[3hzz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3hzz' size='340' side='right'caption='[[3hzz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hzz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1623 As 4.1623]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hzz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_collinus Streptomyces collinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HZZ FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ccr, crotonyl COA reductase ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=42684 AS 4.1623])</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=3hzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hzz OCA], [https://pdbe.org/3hzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hzz RCSB], [https://www.ebi.ac.uk/pdbsum/3hzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hzz ProSAT]</span></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=3hzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hzz OCA], [https://pdbe.org/3hzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hzz RCSB], [https://www.ebi.ac.uk/pdbsum/3hzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hzz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCR_STRCU CCR_STRCU] May play a role in supplying butyryl-CoA for straight-chain fatty acid biosynthesis. Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It shows a high substrate specificity for crotonyl-CoA, a short-chain-length (C4), but no measurable activity is observed with shorter (C3) or longer-chain-length enoyl-CoA thioesters.<ref>PMID:8521864</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3hzz ConSurf].
</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=3hzz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chemo- and stereoselective reductions are important reactions in chemistry and biology, and reductases from biological sources are increasingly applied in organic synthesis. In contrast, carboxylases are used only sporadically. We recently described crotonyl-CoA carboxylase/reductase, which catalyzes the reduction of (E)-crotonyl-CoA to butyryl-CoA but also the reductive carboxylation of (E)-crotonyl-CoA to ethylmalonyl-CoA. In this study, the complete stereochemical course of both reactions was investigated in detail. The pro-(4R) hydrogen of NADPH is transferred in both reactions to the re face of the C3 position of crotonyl-CoA. In the course of the carboxylation reaction, carbon dioxide is incorporated in anti fashion at the C2 atom of crotonyl-CoA. For the reduction reaction that yields butyryl-CoA, a solvent proton is added in anti fashion instead of the CO(2). Amino acid sequence analysis showed that crotonyl-CoA carboxylase/reductase is a member of the medium-chain dehydrogenase/reductase superfamily and shares the same phylogenetic origin. The stereospecificity of the hydride transfer from NAD(P)H within this superfamily is highly conserved, although the substrates and reduction reactions catalyzed by its individual representatives differ quite considerably. Our findings led to a reassessment of the stereospecificity of enoyl(-thioester) reductases and related enzymes with respect to their amino acid sequence, revealing a general pattern of stereospecificity that allows the prediction of the stereochemistry of the hydride transfer for enoyl reductases of unknown specificity. Further considerations on the reaction mechanism indicated that crotonyl-CoA carboxylase/reductase may have evolved from enoyl-CoA reductases. This may be useful for protein engineering of enoyl reductases and their application in biocatalysis.
Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase.,Erb TJ, Brecht V, Fuchs G, Muller M, Alber BE Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8871-6. Epub 2009 May 20. PMID:19458256<ref>PMID:19458256</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hzz" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1623]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Musayev, F N]]
[[Category: Streptomyces collinus]]
[[Category: Scarsdale, J N]]
[[Category: Musayev FN]]
[[Category: Wright, H T]]
[[Category: Scarsdale JN]]
[[Category: Acetyl coa assimilation]]
[[Category: Wright HT]]
[[Category: Alcohol dehydrogenase]]
[[Category: Biocatalysis]]
[[Category: Carboxylase]]
[[Category: Enoyl reductase]]
[[Category: Glyoxolate cycle]]
[[Category: Methylotrophy]]
[[Category: Oxidoreductase]]
[[Category: Polyketide]]
[[Category: Reductase]]
[[Category: Serine cycle]]

Latest revision as of 13:02, 21 February 2024

2.4 Angstrom Crystal Structure of Streptomyces collinus crotonyl CoA carboxylase/reductase2.4 Angstrom Crystal Structure of Streptomyces collinus crotonyl CoA carboxylase/reductase

Structural highlights

3hzz is a 4 chain structure with sequence from Streptomyces collinus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CCR_STRCU May play a role in supplying butyryl-CoA for straight-chain fatty acid biosynthesis. Catalyzes the conversion of crotonyl-CoA to butyryl-CoA. It shows a high substrate specificity for crotonyl-CoA, a short-chain-length (C4), but no measurable activity is observed with shorter (C3) or longer-chain-length enoyl-CoA thioesters.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Wallace KK, Bao ZY, Dai H, Digate R, Schuler G, Speedie MK, Reynolds KA. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur J Biochem. 1995 Nov 1;233(3):954-62. PMID:8521864 doi:10.1111/j.1432-1033.1995.954_3.x

3hzz, resolution 2.40Å

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