2v5j: Difference between revisions
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==Apo Class II aldolase HpcH== | ==Apo Class II aldolase HpcH== | ||
<StructureSection load='2v5j' size='340' side='right' caption='[[2v5j]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='2v5j' size='340' side='right'caption='[[2v5j]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v5j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_c Escherichia coli c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5J OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2v5j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_c Escherichia coli c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5J OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2V5J FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v5k|2v5k]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v5k|2v5k]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2v5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5j OCA], [http://pdbe.org/2v5j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v5j RCSB], [http://www.ebi.ac.uk/pdbsum/2v5j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Aldolase|Aldolase]] | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli c]] | [[Category: Escherichia coli c]] | ||
[[Category: Large Structures]] | |||
[[Category: Bugg, T D.H]] | [[Category: Bugg, T D.H]] | ||
[[Category: Fulop, V]] | [[Category: Fulop, V]] | ||
Revision as of 14:20, 17 June 2020
Apo Class II aldolase HpcHApo Class II aldolase HpcH
Structural highlights
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 PubMedMicroorganisms are adept at degrading chemically resistant aromatic compounds. One of the longest and most well characterized aromatic catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway of Escherichia coli. The final step involves the conversion of 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic semialdehyde. This reaction is catalyzed by 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the divalent metal ion dependent class II aldolase enzymes that have great biosynthetic potential. We have solved the crystal structure of HpcH in the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues. Structure and mechanism of HpcH: a metal ion dependent class II aldolase from the homoprotocatechuate degradation pathway of Escherichia coli.,Rea D, Fulop V, Bugg TD, Roper DI J Mol Biol. 2007 Nov 2;373(4):866-76. Epub 2007 Jun 26. PMID:17881002[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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