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4qvg

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'''Unreleased structure'''
 
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The entry 4qvg is ON HOLD until Paper Publication
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==Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in its apo form==
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<StructureSection load='4qvg' size='340' side='right'caption='[[4qvg]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4qvg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptosporangium_sibiricum Streptosporangium sibiricum]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QVG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qvg OCA], [https://pdbe.org/4qvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qvg RCSB], [https://www.ebi.ac.uk/pdbsum/4qvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qvg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C0LTM6_STRSJ C0LTM6_STRSJ]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Liu, J.S., Chen, S.C., Huang, C.H., Yang, C.S., Chen, Y.
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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>
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Description: Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in its apo form
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Liu, J.S]]
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<div class="pdbe-citations 4qvg" style="background-color:#fffaf0;"></div>
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[[Category: Chen, Y]]
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== References ==
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[[Category: Huang, C.H]]
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<references/>
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[[Category: Chen, S.C]]
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__TOC__
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[[Category: Yang, C.S]]
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptosporangium sibiricum]]
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[[Category: Chen SC]]
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[[Category: Chen Y]]
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[[Category: Huang CH]]
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[[Category: Liu JS]]
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[[Category: Yang CS]]

Current revision

Crystal structure of S-adenosylmethionine-dependent methyltransferase SibL in its apo form

PDB ID 4qvg

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