2v5k
From Proteopedia
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| - | [[Image:2v5k.jpg|left|200px]] | + | [[Image:2v5k.jpg|left|200px]] |
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| - | '''CLASS II ALDOLASE HPCH- MAGNESIUM- OXAMATE COMPLEX''' | + | {{Structure |
| + | |PDB= 2v5k |SIZE=350|CAPTION= <scene name='initialview01'>2v5k</scene>, resolution 2.20Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Oxm+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Oxm+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Po4+Binding+Site+For+Chain+A'>AC5</scene> and <scene name='pdbsite=AC6:Po4+Binding+Site+For+Chain+B'>AC6</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=OXM:OXAMIC ACID'>OXM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CLASS II ALDOLASE HPCH- MAGNESIUM- OXAMATE COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2V5K is a [ | + | 2V5K is a [[Single protein]] structure of 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=2V5K OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17881002 17881002] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:43:13 2008'' |
Revision as of 16:43, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CLASS II ALDOLASE HPCH- MAGNESIUM- OXAMATE COMPLEX
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, coupled with site-directed mutagenesis data, implicate histidine 45 and arginine 70 as key catalytic residues.
About this Structure
2V5K is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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