4gsa

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[[Image:4gsa.gif|left|200px]]<br />
 
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<applet load="4gsa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="4gsa, resolution 2.50&Aring;" />
 
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'''CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE==
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The three-dimensional structure of glutamate-1-semialdehyde aminomutase, (EC 5.4.3.8), an alpha2-dimeric enzyme from Synechococcus, has been, determined by x-ray crystallography using heavy atom derivative phasing., The structure, refined at 2.4-A resolution to an R-factor of 18.7% and, good stereochemistry, explains many of the enzyme's unusual specificity, and functional properties. The overall fold is that of aspartate, aminotransferase and related B6 enzymes, but it also has specific, features. The structure of the complex with gabaculine, a substrate, analogue, shows unexpectedly that the substrate binding site involves, residues from the N-terminal domain of the molecule, notably Arg-32., Glu-406 is suitably positioned to repel alpha-carboxylic acids, thereby, suggesting a basis for the enzyme's reaction specificity. The subunits, show asymmetry in cofactor binding and in the mobilities of the residues, 153-181. In the unliganded enzyme, one subunit has the cofactor bound as, an aldimine of pyridoxal phosphate with Lys-273 and, in this subunit, residues 153-181 are disordered. In the other subunit in which the, cofactor is not covalently bound, residues 153-181 are well defined., Consistent with the crystallographically demonstrated asymmetry, a form of, the enzyme in which both subunits have pyridoxal phosphate bound to, Lys-273 through a Schiff base showed biphasic reduction by borohydride in, solution. Analysis of absorption spectra during reduction provided, evidence of communication between the subunits. The crystal structure of, the reduced form of the enzyme shows that, despite identical cofactor, binding in each monomer, the structural asymmetry at residues 153-181, remains.
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<StructureSection load='4gsa' size='340' side='right'caption='[[4gsa]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4gsa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GSA 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=4gsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gsa OCA], [https://pdbe.org/4gsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gsa RCSB], [https://www.ebi.ac.uk/pdbsum/4gsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gsa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSA_SYNP6 GSA_SYNP6]
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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/gs/4gsa_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=4gsa 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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4GSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with PLP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamate-1-semialdehyde_2,1-aminomutase Glutamate-1-semialdehyde 2,1-aminomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.3.8 5.4.3.8] Structure known Active Sites: COA and COB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4GSA OCA].
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*[[Aminomutase 3D structures|Aminomutase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity., Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN, Proc Natl Acad Sci U S A. 1997 May 13;94(10):4866-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9144156 9144156]
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[[Category: Large Structures]]
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[[Category: Glutamate-1-semialdehyde 2,1-aminomutase]]
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[[Category: Synechococcus sp]]
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[[Category: Single protein]]
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[[Category: Hennig M]]
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[[Category: Synechococcus sp.]]
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[[Category: Jansonius JN]]
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[[Category: Hennig, M.]]
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[[Category: Jansonius, J.N.]]
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[[Category: PLP]]
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[[Category: asymmetric dimer]]
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[[Category: chlorophyll biosynthesis]]
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[[Category: pyridoxal-5'-phosphate]]
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[[Category: pyridoxamine-5'-phosphate]]
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[[Category: reduced form]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:17:21 2007''
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Current revision

CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE

PDB ID 4gsa

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