1brm

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(New page: 200px<br /> <applet load="1brm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1brm, resolution 2.5&Aring;" /> '''ASPARTATE BETA-SEMIA...)
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[[Image:1brm.gif|left|200px]]<br />
 
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<applet load="1brm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1brm, resolution 2.5&Aring;" />
 
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'''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI'''<br />
 
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==Overview==
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==ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10369777 (full description)]]
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<StructureSection load='1brm' size='340' side='right'caption='[[1brm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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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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</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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<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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</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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==About this Structure==
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==See Also==
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1BRM is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BRM OCA]].
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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== References ==
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==Reference==
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<references/>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10369777 10369777]
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__TOC__
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</StructureSection>
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:00:17 2007''
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Current revision

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI

PDB ID 1brm

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