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5dk6

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CRYSTAL STRUCTURE OF A 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE (MTA/SAH) NUCLEOSIDASE (MTAN) FROM COLWELLIA PSYCHRERYTHRAEA 34H (CPS_4743, TARGET PSI-029300) IN COMPLEX WITH ADENINE AT 2.27 A RESOLUTION

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Retrieved from "http://52.214.119.220/wiki/index.php/5dk6"

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 <StructureSection load='5dk6' size='340' side='right'caption='[[5dk6]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dk6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Colp3 Colp3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DK6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DK6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dk6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Colwellia_psychrerythraea_34H Colwellia psychrerythraea 34H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DK6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DK6 FirstGlance]. <br>
-</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=GLY:GLYCINE'>GLY</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]] 2.27&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wkb|4wkb]], [[4x24|4x24]], [[3dp9|3dp9]], [[4g89|4g89]], [[4qez|4qez]]</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=5dk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dk6 OCA], [https://pdbe.org/5dk6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dk6 RCSB], [https://www.ebi.ac.uk/pdbsum/5dk6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dk6 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtnN, CPS_4743 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=167879 COLP3])</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'>[http://proteopedia.org/fgij/fg.htm?mol=5dk6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dk6 OCA], [http://pdbe.org/5dk6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dk6 RCSB], [http://www.ebi.ac.uk/pdbsum/5dk6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dk6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MTNN_COLP3 MTNN_COLP3]] 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.[HAMAP-Rule:MF_01684]
+[https://www.uniprot.org/uniprot/MTNN_COLP3 MTNN_COLP3] 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.[HAMAP-Rule:MF_01684]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-'-Methylthioadenosine/S-adenosyl-l-homocysteine nucleosidases (MTANs) catalyze the hydrolysis of 5'-methylthioadenosine to adenine and 5-methylthioribose. The amino acid sequences of the MTANs from Vibrio cholerae (VcMTAN) and Escherichia coli (EcMTAN) are 60% identical and 75% similar. Protein structure folds and kinetic properties are similar. However, binding of transition-state analogues is dominated by favorable entropy in VcMTAN and by enthalpy in EcMTAN. Catalytic sites of VcMTAN and EcMTAN in contact with reactants differ by two residues; Ala113 and Val153 in VcMTAN are Pro113 and Ile152, respectively, in EcMTAN. We mutated the VcMTAN catalytic site residues to match those of EcMTAN in anticipation of altering its properties toward EcMTAN. Inhibition of VcMTAN by transition-state analogues required filling both active sites of the homodimer. However, in the Val153Ile mutant or double mutants, transition-state analogue binding at one site caused complete inhibition. Therefore, a single amino acid, Val153, alters the catalytic site cooperativity in VcMTAN. The transition-state analogue affinity and thermodynamics in mutant VcMTAN became even more unlike those of EcMTAN, the opposite of expectations from catalytic site similarity; thus, catalytic site contacts in VcMTAN are unable to recapitulate the properties of EcMTAN. X-ray crystal structures of EcMTAN, VcMTAN, and a multiple-site mutant of VcMTAN most closely resembling EcMTAN in catalytic site contacts show no major protein conformational differences. The overall protein architectures of these closely related proteins are implicated in contributing to the catalytic site differences.
-Active site and remote contributions to catalysis in methylthioadenosine nucleosidases.,Thomas K, Cameron SA, Almo SC, Burgos ES, Gulab SA, Schramm VL Biochemistry. 2015 Apr 21;54(15):2520-9. doi: 10.1021/bi501487w. Epub 2015 Apr 3. PMID:25806409<ref>PMID:25806409</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5dk6" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Adenosylhomocysteine nucleosidase]]
+[[Category: Colwellia psychrerythraea 34H]]
-[[Category: Colp3]]
 [[Category: Large Structures]]
-[[Category: Ahmed, M]]
+[[Category: Ahmed M]]
-[[Category: Almo, S C]]
+[[Category: Almo SC]]
-[[Category: Bhosle, R]]
+[[Category: Bhosle R]]
-[[Category: Bonanno, J B]]
+[[Category: Bonanno JB]]
-[[Category: Celikgil, A]]
+[[Category: Celikgil A]]
-[[Category: Chamala, S]]
+[[Category: Chamala S]]
-[[Category: Chan, M K]]
+[[Category: Chan MK]]
-[[Category: Evans, B]]
+[[Category: Evans B]]
-[[Category: Fiser, A]]
+[[Category: Fiser A]]
-[[Category: Garforth, S]]
+[[Category: Garforth S]]
-[[Category: Gizzi, A]]
+[[Category: Gizzi A]]
-[[Category: Hillerich, B]]
+[[Category: Hillerich B]]
-[[Category: Himmel, D M]]
+[[Category: Himmel DM]]
-[[Category: Kar, A]]
+[[Category: Kar A]]
-[[Category: Lafluer, J]]
+[[Category: Lafluer J]]
-[[Category: Lim, S]]
+[[Category: Lim S]]
-[[Category: Love, J]]
+[[Category: Love J]]
-[[Category: Matikainen, B]]
+[[Category: Matikainen B]]
-[[Category: Structural genomic]]
+[[Category: Patel H]]
-[[Category: Patel, H]]
+[[Category: Seidel RD]]
-[[Category: Seidel, R D]]
+[[Category: Toro R]]
-[[Category: Toro, R]]
+[[Category: Villegas G]]
-[[Category: Villegas, G]]
-[[Category: Adenine]]
-[[Category: Gammaproteobacteria]]
-[[Category: Hydrolase]]
-[[Category: Mta/sah nucleosidase family]]
-[[Category: Mtan]]
-[[Category: Nysgrc]]
-[[Category: PSI, Protein structure initiative]]
-[[Category: Protein-ligand complex]]
-[[Category: Psi-biology]]
-[[Category: Vibrio psychroerythus]]

5dk6

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF A 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE (MTA/SAH) NUCLEOSIDASE (MTAN) FROM COLWELLIA PSYCHRERYTHRAEA 34H (CPS_4743, TARGET PSI-029300) IN COMPLEX WITH ADENINE AT 2.27 A RESOLUTION

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