5ccd

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m (Protected "5ccd" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5ccd is ON HOLD
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==Joint X-ray/neutron structure of MTAN D198N complex with SAH==
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<StructureSection load='5ccd' size='340' side='right'caption='[[5ccd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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Authors: Banco, M., Kovalevsky, A., Ronning, D.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5ccd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_J99 Helicobacter pylori J99]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CCD FirstGlance]. <br>
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Description: Joint X-ray/neutron structure of MTAN D198N complex with SAH
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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[[Category: Ronning, D]]
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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=5ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccd OCA], [https://pdbe.org/5ccd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ccd RCSB], [https://www.ebi.ac.uk/pdbsum/5ccd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ccd ProSAT]</span></td></tr>
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[[Category: Banco, M]]
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</table>
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[[Category: Kovalevsky, A]]
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== Function ==
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[https://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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Helicobacter pylori J99]]
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[[Category: Large Structures]]
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[[Category: Banco MT]]
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[[Category: Kovalevsky AY]]
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[[Category: Ronning DR]]

Current revision

Joint X-ray/neutron structure of MTAN D198N complex with SAH

PDB ID 5ccd

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