2v5j: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
Microorganisms 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, . | Microorganisms 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. | ||
==About this Structure== | ==About this Structure== | ||
2V5J is a | 2V5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2V5J OCA]. | ||
==Reference== | ==Reference== | ||
| Line 26: | Line 26: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 18:53:27 2007'' | ||
Revision as of 19:48, 5 November 2007
|
APO CLASS II ALDOLASE HPCH
OverviewOverview
Microorganisms 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.
About this StructureAbout this Structure
2V5J is a Single protein structure of sequence from Escherichia coli with PO4 and GOL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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 Jun 26;. PMID:17881002
Page seeded by OCA on Mon Nov 5 18:53:27 2007