3asu: Difference between revisions
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< | ==Crystal structure of serine dehydrogenase from Escherichia coli== | ||
<StructureSection load='3asu' size='340' side='right'caption='[[3asu]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3asu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ASU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ASU 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]] 1.9Å</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=3asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3asu OCA], [https://pdbe.org/3asu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3asu RCSB], [https://www.ebi.ac.uk/pdbsum/3asu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3asu ProSAT]</span></td></tr> | ||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Serine dehydrogenase from Escherichia coli is a homotetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) family. This enzyme catalyses the NADP(+)-dependent oxidation of serine to 2-aminomalonate semialdehyde. The enzyme shows a stereospecificity for beta-(3S)-hydroxy acid as a substrate; however, no stereospecificity was observed at the alpha-carbon. The structures of the ligand-free SerDH and SerDH-NADP(+)-phosphate complex were determined at 1.9 and 2.7 A resolutions, respectively. The overall structure, including the catalytic tetrad of Asn106, Ser134, Tyr147 and Lys151, shows obvious relationships with other members of the SDR family. The structure of the substrate-binding loop and that of the C-terminal region were disordered in the ligand-free enzyme, whereas these structures were clearly defined in the SerDH-NADP(+) complex as a closed form. Interestingly, the C-terminal region was protruded from the main body and it formed an anti-parallel beta-sheet with another C-terminal region on the subunit that is diagonally opposite to that in the tetramer. It is revealed that the C-terminal region possesses the important roles in substrate binding through the stabilization of the substrate-binding loop in the closed form complex. The roles of the C-terminal region along with those of the residues involved in substrate recognition were studied by site-directed mutagenesis. | |||
Crystal structure of serine dehydrogenase from Escherichia coli: important role of the C-terminal region for closed-complex formation.,Yamazawa R, Nakajima Y, Mushiake K, Yoshimoto T, Ito K J Biochem. 2011 Jun;149(6):701-12. Epub 2011 Feb 23. PMID:21349860<ref>PMID:21349860</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3asu" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ito | [[Category: Ito K]] | ||
[[Category: Nakajima | [[Category: Nakajima Y]] | ||
[[Category: Yamazawa | [[Category: Yamazawa R]] | ||
[[Category: Yoshimoto | [[Category: Yoshimoto T]] | ||
Latest revision as of 15:54, 4 October 2023
Crystal structure of serine dehydrogenase from Escherichia coli
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