6ayt: Difference between revisions

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 <StructureSection load='6ayt' size='340' side='right'caption='[[6ayt]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ayt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AYT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ayt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AYT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AYT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4EH:(3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(PYRAZIN-2-YLSULFANYL)METHYL]PYRROLIDIN-3-OL'>4EH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A0M70_07260, AJY53_05400 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4EH:(3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(PYRAZIN-2-YLSULFANYL)METHYL]PYRROLIDIN-3-OL'>4EH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteine_nucleosidase Adenosylhomocysteine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.9 3.2.2.9] </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=6ayt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ayt OCA], [https://pdbe.org/6ayt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ayt RCSB], [https://www.ebi.ac.uk/pdbsum/6ayt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ayt ProSAT]</span></td></tr>
-<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=6ayt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ayt OCA], [http://pdbe.org/6ayt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ayt RCSB], [http://www.ebi.ac.uk/pdbsum/6ayt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ayt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/A0A1E7P7U4_CAMJU A0A1E7P7U4_CAMJU]] Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively.[SAAS:SAAS00679308]
+[https://www.uniprot.org/uniprot/MQMTN_CAMJE MQMTN_CAMJE] 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 Campylobacter 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. Shows negligible activity with futalosine (FL) as substrate.<ref>PMID:21489995</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 __TOC__
 </StructureSection>
-[[Category: Campylobacter fetus subsp. jejuni smibert 1974]]
+[[Category: Campylobacter jejuni]]
-[[Category: Adenosylhomocysteine nucleosidase]]
 [[Category: Large Structures]]
-[[Category: Almo, S C]]
+[[Category: Almo SC]]
-[[Category: Bonanno, J B]]
+[[Category: Bonanno JB]]
-[[Category: Ducati, R G]]
+[[Category: Ducati RG]]
-[[Category: Harijan, R K]]
+[[Category: Harijan RK]]
-[[Category: Schramm, V L]]
+[[Category: Schramm VL]]
-[[Category: Foodborne disease]]
-[[Category: Hydrolase]]
-[[Category: Mtan enzyme]]
-[[Category: Transferase]]