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Haloperoxidase
From Proteopedia
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| - | <StructureSection load='1qi9' size='400' side='right' scene='' caption='Bromoperoxidase complex with VO4 and I- (purple) ions, [[1qi9]]'> | + | <StructureSection load='1qi9' size='400' side='right' scene='48/486480/Cv/1' caption='Bromoperoxidase complex with VO4 and I- (purple) ions, [[1qi9]]'> |
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The vanadate ion shows a trigonal bipyramidal coordination. The iodine atoms are coordinated to tyrosine residues<ref>PMID:10543953</ref>. | + | The <scene name='48/486480/Cv/5'>vanadate ion shows a trigonal bipyramidal coordination</scene>. The iodine atoms are coordinated to tyrosine residues: <scene name='48/486480/Cv/6'>first coordination site</scene> and <scene name='48/486480/Cv/7'>second coordination site</scene> <ref>PMID:10543953</ref>. Water molecules shown as red spheres. |
</StructureSection> | </StructureSection> | ||
==3D structures of haloperoxidase== | ==3D structures of haloperoxidase== | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | *Vanadium- | + | *Vanadium-dependent chloroperoxidase |
| - | **[[1vnc]], [[1vni]], [[1idq]], [[1idu]] – CiCPO – ''Curvularia inaequalis''<br /> | + | **[[1vnc]], [[1vni]], [[1idq]], [[1idu]] – CiCPO + VO4 – ''Curvularia inaequalis''<br /> |
| - | **[[1vne]], [[1vnf]], [[1vng]], [[1vnh]] – CiCPO (mutant)<br /> | + | **[[1vne]], [[1vnf]], [[1vng]], [[1vnh]] – CiCPO (mutant) + VO4<br /> |
| - | **[[1vns]] – CiCPO | + | **[[1vns]], [[3bb0]] – CiCPO <br /> |
| + | **[[3w35]] – StCPO – ''Streptomyces''<br /> | ||
| + | **[[3w36]] – StCPO + VO4<br /> | ||
| + | **[[5lpc]] – CPO – ''Acaryochloris marina''<br /> | ||
*Heme-containing chloroperoxidase | *Heme-containing chloroperoxidase | ||
**[[1cpo]], [[2cpo]] – LfCPO – ''Leptoxyphium fumago''<br /> | **[[1cpo]], [[2cpo]] – LfCPO – ''Leptoxyphium fumago''<br /> | ||
| - | **[[2civ]] – LfCPO + Br<br /> | + | **[[2civ]], [[2j18]], [[2j19]] – LfCPO + Br<br /> |
**[[2ciw]] – LfCPO + I<br /> | **[[2ciw]] – LfCPO + I<br /> | ||
**[[2cix]] – LfCPO + cyclopentane-dione + Br<br /> | **[[2cix]] – LfCPO + cyclopentane-dione + Br<br /> | ||
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**[[1a8s]] – PfCPO F + propanoic acid – ''Pseudomonas fluorescens''<br /> | **[[1a8s]] – PfCPO F + propanoic acid – ''Pseudomonas fluorescens''<br /> | ||
**[[1a8u]] – PfCPO T + benzoic acid<br /> | **[[1a8u]] – PfCPO T + benzoic acid<br /> | ||
| - | **[[1a88]] - CPO L – ''Streptomyces lividans'' | + | **[[1a88]] - CPO L – ''Streptomyces lividans''<br /> |
| + | **[[4dgq]] – CPO – ''Burkholderia cenocepacia''<br /> | ||
*Metal-free bromoperoxidase | *Metal-free bromoperoxidase | ||
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**[[1a8q]] – SaBPO A1<br /> | **[[1a8q]] – SaBPO A1<br /> | ||
**[[1bro]] - SaBPO A2<br /> | **[[1bro]] - SaBPO A2<br /> | ||
| - | **[[1brt]] – SaBPO A2 (mutant)<br /> | + | **[[1brt]], [[4iq4]], [[4itv]], [[4ivj]], [[4qes]], [[4qf0]], [[4qff]] – SaBPO A2 (mutant)<br /> |
**[[3fob]] – BPO – ''Bacillus anthracis'' | **[[3fob]] – BPO – ''Bacillus anthracis'' | ||
*Vanadium-containing bromoperoxidase | *Vanadium-containing bromoperoxidase | ||
| - | **[[1qi9]] – | + | **[[1qi9]] – AnBPO + I + VO4 – ''Ascophyllum nodosum''<br /> |
| - | **[[1up8]], [[1qhb]] – | + | **[[5aa6]] – AnBPO-2 + VO4<br /> |
| + | **[[1up8]], [[1qhb]], [[7qyy]] – CpBPO – ''Corallina pilulifera''<br /> | ||
| + | **[[7qvw]] – CpBPO (mutant) <br /> | ||
| + | **[[7qwi]] – CpBPO + VO4<br /> | ||
| + | **[[7qw3]] – CpBPO (mutant) + Br<br /> | ||
*Vanadium-containing iodoperoxidase | *Vanadium-containing iodoperoxidase | ||
Current revision
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3D structures of haloperoxidase
Updated on 27-April-2023
References
- ↑ Winter JM, Moore BS. Exploring the chemistry and biology of vanadium-dependent haloperoxidases. J Biol Chem. 2009 Jul 10;284(28):18577-81. doi: 10.1074/jbc.R109.001602. Epub, 2009 Apr 10. PMID:19363038 doi:http://dx.doi.org/10.1074/jbc.R109.001602
- ↑ Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D. X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution. J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953 doi:10.1006/jmbi.1999.3179
