1jmz

<StructureSection load='1jmz' size='340' side='right' caption='[[1jmz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1jmz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JMZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PND:P-NITROPHENYLHYDRAZINE'>PND</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jmx|1jmx]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jmz OCA], [http://pdbe.org/1jmz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jmz RCSB], [http://www.ebi.ac.uk/pdbsum/1jmz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jmz ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/QADG_PSEPU QADG_PSEPU]] Catalyzes the oxidative deamination of a wide range of aliphatic and aromatic amines.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jm/1jmz_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11704672</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jmz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Hirotsu, K]]

[[Category: Miyahara, I]]

[[Category: Satoh, A]]

[[Category: Amine dehydrogenase]]

[[Category: Oxidoreductase]]