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6jnj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (apo-form)== | |
| - | + | <StructureSection load='6jnj' size='340' side='right'caption='[[6jnj]], [[Resolution|resolution]] 1.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6jnj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JNJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JNJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 ATCC 29145])</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=6jnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jnj OCA], [http://pdbe.org/6jnj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jnj RCSB], [http://www.ebi.ac.uk/pdbsum/6jnj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jnj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ARAA_AZOBR ARAA_AZOBR]] Catalyzes the NAD(P)(+)-dependent conversion of L-arabinose to L-arabino-gamma-lactone. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NADP(+) to NAD(+) as electron acceptor. Displays high catalytic efficiency for both L-arabinose and D-galactose in vitro. However, the enzyme appears to be involved in the metabolism of L-arabinose but not D-galactose in vivo. To a lesser extent, is also active on D-talose and D-xylose as substrates in vitro, but not with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose.<ref>PMID:16326697</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Atcc 29145]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Iga, C]] | ||
| + | [[Category: Watanabe, S]] | ||
| + | [[Category: Watanabe, Y]] | ||
| + | [[Category: Gfo/idh/moca protein family]] | ||
| + | [[Category: L-arabinose metabolism]] | ||
| + | [[Category: Nadp-dependent dehydrogenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:30, 21 May 2019
Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (apo-form)
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