1jmx
From Proteopedia
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|PDB= 1jmx |SIZE=350|CAPTION= <scene name='initialview01'>1jmx</scene>, resolution 1.9Å | |PDB= 1jmx |SIZE=350|CAPTION= <scene name='initialview01'>1jmx</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> | + | |LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jmz|1JMZ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmx OCA], [http://www.ebi.ac.uk/pdbsum/1jmx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jmx RCSB]</span> | ||
}} | }} | ||
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[[Category: Miyahara, I.]] | [[Category: Miyahara, I.]] | ||
[[Category: Satoh, A.]] | [[Category: Satoh, A.]] | ||
| - | [[Category: HEC]] | ||
| - | [[Category: NI]] | ||
[[Category: amine dehydrogenase]] | [[Category: amine dehydrogenase]] | ||
| - | ''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 21:35:56 2008'' |
Revision as of 18:35, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1JMZ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
crystal structure of a quinohemoprotein amine dehydrogenase from pseudomonas putida
Overview
The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure.
About this Structure
1JMX is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges., Satoh A, Kim JK, Miyahara I, Devreese B, Vandenberghe I, Hacisalihoglu A, Okajima T, Kuroda S, Adachi O, Duine JA, Van Beeumen J, Tanizawa K, Hirotsu K, J Biol Chem. 2002 Jan 25;277(4):2830-4. Epub 2001 Nov 9. PMID:11704672
Page seeded by OCA on Sun Mar 30 21:35:56 2008
