4cr8: Difference between revisions
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''' | ==Crystal structure of the N-acetyl-D-mannosamine dehydrogenase with NAD== | ||
<StructureSection load='4cr8' size='340' side='right' caption='[[4cr8]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4cr8]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CR8 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cr6|4cr6]], [[4cr7|4cr7]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acylmannosamine_1-dehydrogenase N-acylmannosamine 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.233 1.1.1.233] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cr8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cr8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cr8 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
N-acetyl-D-mannosamine dehydrogenase (NAMDH) from the soil bacteroidete Flavobacterium sp 141-8 catalyses a rare NAD+-dependent oxidation of N-acetyl-D-mannosamine (ManNAc) into N-acetylmannosamino-lactone, which spontaneously hydrolyses into N-acetylmannosaminic acid. NAMDH belongs to the SDR (short-chain dehydrogenase/reductase) superfamily representing the only NAMDH characterized to date. Thorough functional, stability, site-directed mutagenesis and crystallographic studies have been carried out to better understand the structural and biochemical aspects of this unique enzyme. NAMDH exhibited remarkable alkaline pH optimum (pH 9.4) with a high thermal stability in glycine buffer (Tm = 64 masculineC) and a strict selectivity towards ManNAc and NAD+. Crystal structures of ligand-free and N-acetyl-D-mannosamine and NAD+-bound enzyme forms revealed a compact homotetramer having point 222 symmetry, formed by subunits presenting the characteristic SDR alpha3beta7alpha3 sandwich fold. A highly developed C-terminal tail used as a latch connecting nearby subunits stabilizes the tetramer. A dense network of polar interactions with the substrate including the encasement of its acetamido group in a specific binding pocket and the hydrogen binding of the sugar 4OH atom ensure specificity for N-acetyl-D-mannosamine.The NAMDH-substrate complexes and site-directed mutagenesis studies identify the catalytic tetrad and provide useful traits for identifying new NAMDH sequences. | |||
Crystal structures and functional studies clarify substrate selectivity and catalytic residues for the unique orphan enzyme N-acetyl-D-mannosamine dehydrogenase.,Sola-Carvajal A, Gil-Ortiz F, Garcia-Carmona F, Rubio V, Sanchez-Ferrer A Biochem J. 2014 Jun 27. PMID:24969681<ref>PMID:24969681</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: N-acylmannosamine 1-dehydrogenase]] | |||
[[Category: Garcia-Carmona, F.]] | |||
[[Category: Gil-Ortiz, F.]] | |||
[[Category: Rubio, V.]] | |||
[[Category: Sanchez-Ferrer, A.]] | |||
[[Category: Sola-Carvajal, A.]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Short-chain dehydrogenase/reductase]] | |||
[[Category: Substrate selectivity]] | |||
