1brm: Difference between revisions

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 <StructureSection load='1brm' size='340' side='right'caption='[[1brm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1brm]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BRM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1brm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BRM FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.5&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] </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=1brm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brm OCA], [https://pdbe.org/1brm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1brm RCSB], [https://www.ebi.ac.uk/pdbsum/1brm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1brm ProSAT]</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=1brm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1brm OCA], [http://pdbe.org/1brm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1brm RCSB], [http://www.ebi.ac.uk/pdbsum/1brm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1brm ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DHAS_ECOLI DHAS_ECOLI]] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:6102909</ref> <ref>PMID:11368768</ref>
+[https://www.uniprot.org/uniprot/DHAS_ECOLI DHAS_ECOLI] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.<ref>PMID:6102909</ref> <ref>PMID:11368768</ref>
 == 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=1brm ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in an essential aspartic biosynthetic pathway found in bacteria, fungi and the higher plants. Mutations in the asd gene encoding for ASADH that produce an inactive enzyme are lethal, which suggests that ASADH may be an effective target for antibacterial, herbicidal and fungicidal agents.We have solved the crystal structure of the Escherichia coli enzyme to 2.5 A resolution using single isomorphous replacement and 3-fold non-crystallographic symmetry. Each monomer has an N-terminal nucleotide-binding domain and a dimerisation domain. The presence of an essential cysteine locates the active site in a cleft between the two domains. The functional dimer has the appearance of a butterfly, with the NADP-binding domains forming the wings and the dimerisation domain forming the body.A histidine residue is identified as a likely acid/base catalyst in the enzymic reaction. Other amino acids implicated in the enzymic activity by mutagenesis are found in the active site region and define the substrate binding pocket.
-Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis.,Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R J Mol Biol. 1999 Jun 18;289(4):991-1002. PMID:10369777<ref>PMID:10369777</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1brm" style="background-color:#fffaf0;"></div>
 ==See Also==
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 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: Aspartate-semialdehyde dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Hadfield, A T]]
+[[Category: Hadfield AT]]
-[[Category: Kryger, G]]
+[[Category: Kryger G]]
-[[Category: Ouyang, J]]
+[[Category: Ouyang J]]
-[[Category: Petsko, G A]]
+[[Category: Petsko GA]]
-[[Category: Ringe, D]]
+[[Category: Ringe D]]
-[[Category: Viola, R E]]
+[[Category: Viola RE]]
-[[Category: Dehydrogenase]]
-[[Category: Enzyme]]
-[[Category: Escherichia coli]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]