2h88

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|PDB= 2h88 |SIZE=350|CAPTION= <scene name='initialview01'>2h88</scene>, resolution 1.74&Aring;
|PDB= 2h88 |SIZE=350|CAPTION= <scene name='initialview01'>2h88</scene>, resolution 1.74&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=BHG:2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>BHG</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene>, <scene name='pdbligand=UNL:'>UNL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=BHG:2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL'>BHG</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(ubiquinone) Succinate dehydrogenase (ubiquinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(ubiquinone) Succinate dehydrogenase (ubiquinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </span>
|GENE=
|GENE=
 +
|DOMAIN=
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|RELATEDENTRY=[[2fbw|2FBW]], [[1yq3|1YQ3]], [[1yq4|1YQ4]], [[1zoy|1ZOY]], [[1zpo|1ZPO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h88 OCA], [http://www.ebi.ac.uk/pdbsum/2h88 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h88 RCSB]</span>
}}
}}
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[[Category: Shen, J T.]]
[[Category: Shen, J T.]]
[[Category: Wang, A C.]]
[[Category: Wang, A C.]]
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[[Category: AZI]]
 
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[[Category: BHG]]
 
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[[Category: F3S]]
 
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[[Category: FAD]]
 
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[[Category: FES]]
 
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[[Category: GOL]]
 
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[[Category: HEM]]
 
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[[Category: K]]
 
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[[Category: SF4]]
 
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[[Category: TEO]]
 
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[[Category: UNL]]
 
[[Category: complex ii]]
[[Category: complex ii]]
[[Category: cytochrome b]]
[[Category: cytochrome b]]
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[[Category: ubiquinone]]
[[Category: ubiquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:13:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:26:50 2008''

Revision as of 00:26, 31 March 2008


PDB ID 2h88

Drag the structure with the mouse to rotate
, resolution 1.74Å
Ligands: , , , , , , , , , ,
Activity: Succinate dehydrogenase (ubiquinone), with EC number 1.3.5.1
Related: 2FBW, 1YQ3, 1YQ4, 1ZOY, 1ZPO


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Avian Mitochondrial Respiratory Complex II at 1.8 Angstrom Resolution


Overview

Mitochondrial Complex II (succinate:ubiquinone oxidoreductase) is purified in a partially inactivated state, which can be activated by removal of tightly bound oxaloacetate (E.B. Kearney, et al., Biochem. Biophys. Res. Commun. 49 1115-1121). We crystallized Complex II in the presence of oxaloacetate or with the endogenous inhibitor bound. The structure showed a ligand essentially identical to the "malate-like intermediate" found in Shewanella Flavocytochrome c crystallized with fumarate (P. Taylor, et al., Nat. Struct. Biol. 6 1108-1112) Crystallization of Complex II in the presence of excess fumarate also gave the malate-like intermediate or a mixture of that and fumarate at the active site. In order to more conveniently monitor the occupation state of the dicarboxylate site, we are developing a library of UV/Vis spectral effects induced by binding different ligands to the site. Treatment with fumarate results in rapid development of the fumarate difference spectrum and then a very slow conversion into a species spectrally similar to the OAA-liganded complex. Complex II is known to be capable of oxidizing malate to the enol form of oxaloacetate (Y.O. Belikova, et al., Biochim. Biophys. Acta 936 1-9). The observations above suggest it may also be capable of interconverting fumarate and malate. It may be useful for understanding the mechanism and regulation of the enzyme to identify the malate-like intermediate and its pathway of formation from oxaloacetate or fumarate.

About this Structure

2H88 is a Protein complex structure of sequences from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the "oxaloacetate-inhibited" state., Huang LS, Shen JT, Wang AC, Berry EA, Biochim Biophys Acta. 2006 Sep-Oct;1757(9-10):1073-83. Epub 2006 Jul 12. PMID:16935256

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