1iwb

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|PDB= 1iwb |SIZE=350|CAPTION= <scene name='initialview01'>1iwb</scene>, resolution 1.85&Aring;
|PDB= 1iwb |SIZE=350|CAPTION= <scene name='initialview01'>1iwb</scene>, resolution 1.85&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=B12:COBALAMIN'>B12</scene>
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|LIGAND= <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Propanediol_dehydratase Propanediol dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.28 4.2.1.28]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Propanediol_dehydratase Propanediol dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.28 4.2.1.28] </span>
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1dio|1DIO]], [[1eex|1EEX]], [[1egm|1EGM]], [[1egv|1EGV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwb OCA], [http://www.ebi.ac.uk/pdbsum/1iwb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iwb RCSB]</span>
}}
}}
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[[Category: Toraya, T.]]
[[Category: Toraya, T.]]
[[Category: Yasuoka, N.]]
[[Category: Yasuoka, N.]]
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[[Category: B12]]
 
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[[Category: K]]
 
[[Category: beta-alpha-barrel]]
[[Category: beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:34 2008''

Revision as of 18:25, 30 March 2008


PDB ID 1iwb

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: ,
Activity: Propanediol dehydratase, with EC number 4.2.1.28
Related: 1DIO, 1EEX, 1EGM, 1EGV


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



Crystal structure of diol dehydratase


Overview

Substrate binding triggers catalytic radical formation through the cobalt-carbon bond homolysis in coenzyme B12-dependent enzymes. We have determined the crystal structure of the substrate-free form of Klebsiella oxytoca diol dehydratase*cyanocobalamin complex at 1.85 A resolution. The structure contains two units of the heterotrimer consisting of alpha, beta, and gamma subunits. As compared with the structure of its substrate-bound form, the beta subunits are tilted by approximately 3 degrees and cobalamin is also tilted so that pyrrole rings A and D are significantly lifted up toward the substrate-binding site, whereas pyrrole rings B and C are only slightly lifted up. The structure revealed that the potassium ion in the substrate-binding site of the substrate-free enzyme is also heptacoordinated; that is, two oxygen atoms of two water molecules coordinate to it instead of the substrate hydroxyls. A modeling study in which the structures of both the cobalamin moiety and the adenine ring of the coenzyme were superimposed onto those of the enzyme-bound cyanocobalamin and the adenine ring-binding pocket, respectively, demonstrated that the distortions of the Co-C bond in the substrate-free form are already marked but slightly smaller than those in the substrate-bound form. It was thus strongly suggested that the Co-C bond becomes largely activated (labilized) when the coenzyme binds to the apoenzyme even in the absence of substrate and undergoes homolysis through the substrate-induced conformational changes of the enzyme. Kinetic coupling of Co-C bond homolysis with hydrogen abstraction from the substrate shifts the equilibrium to dissociation.

About this Structure

1IWB is a Protein complex structure of sequences from Klebsiella oxytoca. Full crystallographic information is available from OCA.

Reference

Substrate-induced conformational change of a coenzyme B12-dependent enzyme: crystal structure of the substrate-free form of diol dehydratase., Shibata N, Masuda J, Morimoto Y, Yasuoka N, Toraya T, Biochemistry. 2002 Oct 22;41(42):12607-17. PMID:12379103

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