5cce
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Joint X-ray/neutron structure of wild type MTAN complexed with SRH and adenine== | |
| - | + | <StructureSection load='5cce' size='340' side='right' caption='[[5cce]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5cce]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2WP:(2S)-2-AMINO-4-({[(2S,3S,4R,5S)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL}SULFANYL)BUTANOIC+ACID'>2WP</scene>, <scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=D8U:DEUTERIUM(1+)'>D8U</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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=5cce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cce OCA], [http://pdbe.org/5cce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cce RCSB], [http://www.ebi.ac.uk/pdbsum/5cce PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cce 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: Binding site]] | ||
| + | [[Category: Deuterium]] | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: N-glycosyl neutron]] | ||
| + | [[Category: Nucleosidase]] | ||
| + | [[Category: S-adenosylhomocysteine]] | ||
Revision as of 03:20, 10 December 2016
Joint X-ray/neutron structure of wild type MTAN complexed with SRH and adenine
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