6jnk

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m (Protected "6jnk" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6jnk is ON HOLD
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==Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (NADP-bound form)==
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<StructureSection load='6jnk' size='340' side='right'caption='[[6jnk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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Authors: Watanabe, Y., Iga, C., Watanabe, S.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6jnk]] is a 4 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=6JNK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JNK FirstGlance]. <br>
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Description: Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (NADP-bound form)
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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[[Category: Unreleased Structures]]
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<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>
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<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=6jnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jnk OCA], [http://pdbe.org/6jnk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jnk RCSB], [http://www.ebi.ac.uk/pdbsum/6jnk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jnk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Atcc 29145]]
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[[Category: Large Structures]]
[[Category: Iga, C]]
[[Category: Iga, C]]
[[Category: Watanabe, S]]
[[Category: Watanabe, S]]
[[Category: Watanabe, Y]]
[[Category: Watanabe, Y]]
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[[Category: Gfo/idh/moca protein family]]
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[[Category: L-arabinose metabolism]]
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[[Category: Nadp-dependent dehydrogenase]]
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[[Category: Oxidoreductase]]

Revision as of 07:30, 21 May 2019

Crystal structure of Azospirillum brasilense L-arabinose 1-dehydrogenase (NADP-bound form)

PDB ID 6jnk

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