1idu
From Proteopedia
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|PDB= 1idu |SIZE=350|CAPTION= <scene name='initialview01'>1idu</scene>, resolution 2.24Å | |PDB= 1idu |SIZE=350|CAPTION= <scene name='initialview01'>1idu</scene>, resolution 2.24Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=VO4:VANADATE ION'>VO4</scene> | + | |LIGAND= <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1idq|1IDQ]], [[1vnc|1VNC]], [[1vne|1VNE]], [[1vnf|1VNF]], [[1vng|1VNG]], [[1vnh|1VNH]], [[1vns|1VNS]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1idu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idu OCA], [http://www.ebi.ac.uk/pdbsum/1idu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1idu RCSB]</span> | ||
}} | }} | ||
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[[Category: Prade, L.]] | [[Category: Prade, L.]] | ||
[[Category: Wever, R.]] | [[Category: Wever, R.]] | ||
| - | [[Category: VO4]] | ||
[[Category: peroxide derivative]] | [[Category: peroxide derivative]] | ||
[[Category: two four-helix bundle]] | [[Category: two four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:18:27 2008'' |
Revision as of 18:18, 30 March 2008
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| , resolution 2.24Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Chloride peroxidase, with EC number 1.11.1.10 | ||||||
| Related: | 1IDQ, 1VNC, 1VNE, 1VNF, 1VNG, 1VNH, 1VNS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE PEROXIDE FORM OF THE VANADIUM-CONTAINING CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS
Overview
Implications for the catalytic mechanism of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis have been obtained from the crystal structures of the native and peroxide forms of the enzyme.The X-ray structures have been solved by difference Fourier techniques using the atomic model of the azide chloroperoxidase complex. The 2.03 A crystal structure (R = 19.7%) of the native enzyme reveals the geometry of the intact catalytic vanadium center. The vanadium is coordinated by four non-protein oxygen atoms and one nitrogen (NE2) atom from histidine 496 in a trigonal bipyramidal fashion. Three oxygens are in the equatorial plane and the fourth oxygen and the nitrogen are at the apexes of the bipyramid. In the 2.24 A crystal structure (R = 17.7%) of the peroxide derivate the peroxide is bound to the vanadium in an eta2-fashion after the release of the apical oxygen ligand. The vanadium is coordinated also by 4 non-protein oxygen atoms and one nitrogen (NE2) from histidine 496. The coordination geometry around the vanadium is that of a distorted tetragonal pyramid with the two peroxide oxygens, one oxygen and the nitrogen in the basal plane and one oxygen in the apical position. A mechanism for the catalytic cycle has been proposed based on these X-ray structures and kinetic data.
About this Structure
1IDU is a Single protein structure of sequence from Curvularia inaequalis. Full crystallographic information is available from OCA.
Reference
Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form., Messerschmidt A, Prade L, Wever R, Biol Chem. 1997 Mar-Apr;378(3-4):309-15. PMID:9165086
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