5ccd
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Joint X-ray/neutron structure of MTAN D198N complex with SAH== | |
| - | + | <StructureSection load='5ccd' size='340' side='right' caption='[[5ccd]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ccd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCD FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | |
| - | [[Category: | + | <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=5ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccd OCA], [http://pdbe.org/5ccd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ccd RCSB], [http://www.ebi.ac.uk/pdbsum/5ccd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccd ProSAT]</span></td></tr> |
| - | [[Category: Ronning, D]] | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [[http://www.uniprot.org/uniprot/MQMTN_HELPJ MQMTN_HELPJ]] Catalyzes the direct conversion of aminodeoxyfutalosine (AFL) into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of the N-glycosidic bond; this reaction seems to represent an essential step in the menaquinone biosynthesis pathway in Helicobacter species. Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Can also probably use S-adenosylhomocysteine (SAH) as substrate, leading to adenine and S-ribosylhomocysteine. These other activities highlight the tremendous versatility of the enzyme, which also plays key roles in S-adenosylmethionine recycling and in the biosynthesis of the quorum-sensing molecule autoinducer-2.<ref>PMID:20954236</ref> <ref>PMID:22891633</ref> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Banco, M T]] | ||
| + | [[Category: Kovalevsky, A Y]] | ||
| + | [[Category: Ronning, D R]] | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: N-glycosyl hydrolase]] | ||
| + | [[Category: Neutron]] | ||
| + | [[Category: S-adenosylhomocysteine]] | ||
Revision as of 10:47, 10 December 2016
Joint X-ray/neutron structure of MTAN D198N complex with SAH
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