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4bmx

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Current revision (11:54, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4bmx' size='340' side='right'caption='[[4bmx]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='4bmx' size='340' side='right'caption='[[4bmx]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bmx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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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]] 1.76&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bmy|4bmy]], [[4bmz|4bmz]], [[4bn0|4bn0]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosylhomocysteine_nucleosidase Adenosylhomocysteine nucleosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.9 3.2.2.9] </span></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=4bmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmx OCA], [https://pdbe.org/4bmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmx RCSB], [https://www.ebi.ac.uk/pdbsum/4bmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmx ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmx OCA], [https://pdbe.org/4bmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmx RCSB], [https://www.ebi.ac.uk/pdbsum/4bmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MTNN_HELPY MTNN_HELPY]] Responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) (By similarity).
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[https://www.uniprot.org/uniprot/MQMTN_HELPY MQMTN_HELPY] 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. Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. 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. Does not act on futalosine (FL) as substrate.<ref>PMID:21098241</ref> <ref>PMID:24083939</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Adenosylhomocysteine nucleosidase]]
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[[Category: Helicobacter pylori 26695]]
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[[Category: Campylobacter pylori]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Davies, G J]]
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[[Category: Davies GJ]]
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[[Category: Kim, R Q]]
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[[Category: Kim RQ]]
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[[Category: Offen, W A]]
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[[Category: Offen WA]]
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[[Category: Stubbs, K A]]
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[[Category: Stubbs KA]]
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[[Category: Hydrolase]]
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Current revision

Native structure of futalosine hydrolase of Helicobacter pylori strain 26695

PDB ID 4bmx

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