1brm

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[[Image:1brm.jpg|left|200px]]
 
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{{Structure
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==ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI==
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|PDB= 1brm |SIZE=350|CAPTION= <scene name='initialview01'>1brm</scene>, resolution 2.5&Aring;
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<StructureSection load='1brm' size='340' side='right'caption='[[1brm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AT1:Active+Site+Identified+From+Modified+CYS.+Site+Site_iden+...'>AT1</scene>, <scene name='pdbsite=AT2:Active+Site+Identified+From+Modified+CYS.+Site+Site_iden+...'>AT2</scene> and <scene name='pdbsite=AT3:Active+Site+Identified+From+Modified+CYS'>AT3</scene>
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY= [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]
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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]] 2.5&#8491;</td></tr>
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|GENE= ASD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=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>
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}}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1brm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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'''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI'''
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==See Also==
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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1BRM is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10369777 10369777]
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hadfield, A T.]]
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[[Category: Hadfield AT]]
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[[Category: Kryger, G.]]
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[[Category: Kryger G]]
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[[Category: Ouyang, J.]]
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[[Category: Ouyang J]]
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[[Category: Petsko, G A.]]
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[[Category: Petsko GA]]
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[[Category: Ringe, D.]]
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[[Category: Ringe D]]
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[[Category: Viola, R E.]]
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[[Category: Viola RE]]
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[[Category: crystal structure]]
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[[Category: dehydrogenase]]
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[[Category: enzyme]]
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[[Category: escherichia coli]]
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[[Category: nadp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:14:50 2008''
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Current revision

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI

PDB ID 1brm

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