3afn: Difference between revisions
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< | ==Crystal structure of aldose reductase A1-R complexed with NADP== | ||
<StructureSection load='3afn' size='340' side='right'caption='[[3afn]], [[Resolution|resolution]] 1.63Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3afn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._A1 Sphingomonas sp. A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AFN FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.63Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3afn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3afn OCA], [https://pdbe.org/3afn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3afn RCSB], [https://www.ebi.ac.uk/pdbsum/3afn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3afn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D6RU56_9SPHN D6RU56_9SPHN] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/af/3afn_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3afn ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Sphingomonas sp. A1, alginate is degraded by alginate lyases to its constituent monosaccharides, which are nonenzymatically converted to an alpha-keto acid, namely, 4-deoxy-l-erythro-5-hexoseulose uronic acid (DEH). The properties of the DEH-metabolizing enzyme and its gene in strain A1 were characterized. In the presence of alginate, strain A1 cells inducibly produced an NADPH-dependent DEH reductase (A1-R) in their cytoplasm. Molecular cloning of the enzyme gene indicated that A1-R belonged to the short-chain dehydrogenase/reductase superfamily and catalyzed the conversion of DEH to 2-keto-3-deoxy-d-gluconic acid most efficiently at around pH 7.0 and 50 masculineC. Crystal structures of A1-R and its complex with NADP were determined at around 1.6A resolution by X-ray crystallography. The enzyme consists of three layers (alpha/beta/alpha), with a coenzyme-binding Rossmann fold. NADP is surrounded by positively charged residues, and Gly-38 and Arg-39 are crucial for NADP binding. Site-directed mutagenesis studies suggest that Ser-150, Tyr-164, and Lys-168 located around the Rossmann fold constitute the catalytic triad. To our knowledge, this is the first report on molecular cloning and structure determination of a bacterial DEH reductase responsible for alginate metabolism. | |||
Molecular identification of unsaturated uronate reductase prerequisite for alginate metabolism in Sphingomonas sp. A1.,Takase R, Ochiai A, Mikami B, Hashimoto W, Murata K Biochim Biophys Acta. 2010 May 27. PMID:20685299<ref>PMID:20685299</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3afn" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | |||
[[Category: | *[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]] | ||
[[Category: Sphingomonas sp.]] | == References == | ||
[[Category: Hashimoto | <references/> | ||
[[Category: Mikami | __TOC__ | ||
[[Category: Murata | </StructureSection> | ||
[[Category: Ochiai | [[Category: Large Structures]] | ||
[[Category: Takase | [[Category: Sphingomonas sp. A1]] | ||
[[Category: Hashimoto W]] | |||
[[Category: Mikami B]] | |||
[[Category: Murata K]] | |||
[[Category: Ochiai A]] | |||
[[Category: Takase R]] |