1lu9: Difference between revisions

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 <StructureSection load='1lu9' size='340' side='right'caption='[[1lu9]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lu9]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Metea Metea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LU9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LU9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lu9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens_AM1 Methylorubrum extorquens AM1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LU9 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lua|1lua]]</div></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]] 1.9&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mtdA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272630 METEA])</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=1lu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu9 OCA], [https://pdbe.org/1lu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lu9 RCSB], [https://www.ebi.ac.uk/pdbsum/1lu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lu9 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylenetetrahydrofolate_dehydrogenase_(NADP(+)) Methylenetetrahydrofolate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.5 1.5.1.5] </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=1lu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lu9 OCA], [http://pdbe.org/1lu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lu9 RCSB], [http://www.ebi.ac.uk/pdbsum/1lu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lu9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MTDA_METEA MTDA_METEA]] Catalyzes the dehydrogenation of methylene-H(4)MPT. Can also catalyze the reversible dehydrogenation of methylene-H(4)F with 20-fold lower catalytic efficiency.
+[https://www.uniprot.org/uniprot/MTDA_METEA MTDA_METEA] Catalyzes the dehydrogenation of methylene-H(4)MPT. Can also catalyze the reversible dehydrogenation of methylene-H(4)F with 20-fold lower catalytic efficiency.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lu9 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-NADP-dependent methylene-H(4)MPT dehydrogenase, MtdA, from Methylobacterium extorquens AM1 catalyzes the dehydrogenation of methylene-tetrahydromethanopterin and methylene-tetrahydrofolate with NADP(+) as cosubstrate. The X-ray structure of MtdA with and without NADP bound was established at 1.9 A resolution. The enzyme is present as a homotrimer. The alpha,beta fold of the monomer is related to that of methylene-H(4)F dehydrogenases, suggesting a common evolutionary origin. The position of the active site is located within a large crevice built up by the two domains of one subunit and one domain of a second subunit. Methylene-H(4)MPT could be modeled into the cleft, and crucial active site residues such as Phe18, Lys256, His260, and Thr102 were identified. The molecular basis of the different substrate specificities and different catalytic demands of MtdA compared to methylene-H(4)F dehydrogenases are discussed.
-Structure of methylene-tetrahydromethanopterin dehydrogenase from methylobacterium extorquens AM1.,Ermler U, Hagemeier CH, Roth A, Demmer U, Grabarse W, Warkentin E, Vorholt JA Structure. 2002 Aug;10(8):1127-37. PMID:12176390<ref>PMID:12176390</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1lu9" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Metea]]
+[[Category: Methylorubrum extorquens AM1]]
-[[Category: Demmer, U]]
+[[Category: Demmer U]]
-[[Category: Ermler, U]]
+[[Category: Ermler U]]
-[[Category: Grabarse, W]]
+[[Category: Grabarse W]]
-[[Category: Hagemeier, C H]]
+[[Category: Hagemeier CH]]
-[[Category: Roth, A]]
+[[Category: Roth A]]
-[[Category: Vorholt, J A]]
+[[Category: Vorholt JA]]
-[[Category: Warkentin, E]]
+[[Category: Warkentin E]]
-[[Category: Alpha/beta twisted open sheet structure]]
-[[Category: Oxidoreductase]]