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==Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia coli K12 substr. MG1655==
==Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia coli K12 substr. MG1655==
<StructureSection load='3mog' size='340' side='right' caption='[[3mog]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3mog' size='340' side='right' caption='[[3mog]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mog]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MOG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mog]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MOG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MOG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paaH, ydbU, b1395, JW1390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">paaH, ydbU, b1395, JW1390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxybutyryl-CoA_dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.157 1.1.1.157] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxybutyryl-CoA_dehydrogenase 3-hydroxybutyryl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.157 1.1.1.157] </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=3mog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mog OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mog RCSB], [http://www.ebi.ac.uk/pdbsum/3mog 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=3mog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mog OCA], [http://pdbe.org/3mog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mog RCSB], [http://www.ebi.ac.uk/pdbsum/3mog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mog ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=3mog ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
== References ==
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</StructureSection>
</StructureSection>
[[Category: 3-hydroxybutyryl-CoA dehydrogenase]]
[[Category: 3-hydroxybutyryl-CoA dehydrogenase]]
[[Category: Escherichia coli]]
[[Category: Ecoli]]
[[Category: Almo, S C]]
[[Category: Almo, S C]]
[[Category: Burley, S K]]
[[Category: Burley, S K]]

Revision as of 23:47, 5 August 2016

Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia coli K12 substr. MG1655Crystal structure of 3-hydroxybutyryl-CoA dehydrogenase from Escherichia coli K12 substr. MG1655

Structural highlights

3mog is a 3 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:paaH, ydbU, b1395, JW1390 (ECOLI)
Activity:3-hydroxybutyryl-CoA dehydrogenase, with EC number 1.1.1.157
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PAAH_ECOLI] Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
  2. ↑ Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14390-5. doi:, 10.1073/pnas.1005399107. Epub 2010 Jul 21. PMID:20660314 doi:10.1073/pnas.1005399107

3mog, resolution 2.20Å

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