5ccd: Difference between revisions

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'''Unreleased structure'''


The entry 5ccd is ON HOLD  until Dec 31 2017
==Joint X-ray/neutron structure of MTAN D198N complex with SAH==
 
<StructureSection load='5ccd' size='340' side='right' caption='[[5ccd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
Authors: Banco, M., Kovalevsky, A., Ronning, D.
== 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>
Description: Joint X-ray/neutron structure of MTAN D198N complex with SAH
</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: Unreleased Structures]]
<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: Banco, M]]
== Function ==
[[Category: Kovalevsky, A]]
[[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

5ccd, resolution 2.20Å

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