4qvg
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in its apo form== |
+ | <StructureSection load='4qvg' size='340' side='right' caption='[[4qvg]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4qvg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QVG FirstGlance]. <br> | ||
+ | </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=4qvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qvg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qvg RCSB], [http://www.ebi.ac.uk/pdbsum/4qvg PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Streptosporangium sibiricum SibL catalyzes the methyl transfer from S-adenosylmethionine (SAM) to 3-hydroxykynurenine (3-HK) to produce S-adenosylhomocysteine (SAH) and 3-hydroxy-4-methyl-kynurenine for sibiromycin biosynthesis. Here, we present the crystal structures of apo-form Ss-SibL, Ss-SibL/SAH binary complex and Ss-SibL/SAH/3-HK ternary complex. Ss-SibL is a homodimer. Each subunit comprises a helical N-terminal domain and a Rossmann-fold C-terminal domain. SAM (or SAH) binding alone results in domain movements, suggesting a two-step catalytic cycle. Analyses of the enzyme-ligand interactions and further mutant studies support a mechanism in which Tyr134 serves as the principal base in the transferase reaction of methyl group from SAM to 3-HK. | ||
- | + | Structure and mechanism of an antibiotics-synthesizing 3-hydroxykynurenine C-methyltransferase.,Chen SC, Huang CH, Lai SJ, Liu JS, Fu PK, Tseng ST, Yang CS, Lai MC, Ko TP, Chen Y Sci Rep. 2015 May 11;5:10100. doi: 10.1038/srep10100. PMID:25960001<ref>PMID:25960001</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | [[Category: | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Chen, S C]] | ||
[[Category: Chen, Y]] | [[Category: Chen, Y]] | ||
- | [[Category: Huang, C | + | [[Category: Huang, C H]] |
- | [[Category: | + | [[Category: Liu, J S]] |
- | [[Category: Yang, C | + | [[Category: Yang, C S]] |
+ | [[Category: Methyltransferase]] | ||
+ | [[Category: Transferase]] |
Revision as of 15:49, 27 May 2015
Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in its apo form
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