1gso

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(New page: 200px<br /><applet load="1gso" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gso, resolution 1.6&Aring;" /> '''GLYCINAMIDE RIBONUCLE...)
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[[Image:1gso.gif|left|200px]]<br /><applet load="1gso" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gso, resolution 1.6&Aring;" />
 
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'''GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.'''<br />
 
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==Overview==
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==GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.==
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Glycinamide ribonucleotide synthetase (GAR-syn) catalyzes the second step, of the de novo purine biosynthetic pathway; the conversion of, phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi. GAR-syn containing an N-terminal polyhistidine tag was, expressed as the SeMet incorporated protein for crystallographic studies., In addition, the protein as isolated contains a Pro294Leu mutation. This, protein was crystallized, and the structure solved using, multiple-wavelength anomalous diffraction (MAD) phase determination and, refined to 1.6 A resolution. GAR-syn adopts an alpha/beta structure that, consists of four domains labeled N, A, B, and C. The N, A, and C domains, are clustered to form a large central core structure whereas the smaller B, domain is extended outward. Two hinge regions, which might readily, facilitate interdomain movement, connect the B domain and the main core. A, search of structural databases showed that the structure of GAR-syn is, similar to D-alanine:D-alanine ligase, biotin carboxylase, and glutathione, synthetase, despite low sequence similarity. These four enzymes all, utilize similar ATP-dependent catalytic mechanisms even though they, catalyze different chemical reactions. Another ATP-binding enzyme with low, sequence similarity but unknown function, synapsin Ia, was also found to, share high structural similarity with GAR-syn. Interestingly, the GAR-syn, N domain shows similarity to the N-terminal region of glycinamide, ribonucleotide transformylase and several dinucleotide-dependent, dehydrogenases. Models of ADP and GAR binding were generated based on, structure and sequence homology. On the basis of these models, the active, site lies in a cleft between the large domain and the extended B domain., Most of the residues that facilitate ATP binding belong to the A or B, domains. The N and C domains appear to be largely responsible for, substrate specificity. The structure of GAR-syn allows modeling studies of, possible channeling complexes with PPRP amidotransferase.
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<StructureSection load='1gso' size='340' side='right'caption='[[1gso]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1gso]] is a 1 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=1GSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSO FirstGlance]. <br>
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1GSO 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/Phosphoribosylamine--glycine_ligase Phosphoribosylamine--glycine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.13 6.3.4.13] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSO OCA].
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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]] 1.6&#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=1gso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gso OCA], [https://pdbe.org/1gso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gso RCSB], [https://www.ebi.ac.uk/pdbsum/1gso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gso ProSAT]</span></td></tr>
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==Reference==
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</table>
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X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli., Wang W, Kappock TJ, Stubbe J, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15647-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9843369 9843369]
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== Function ==
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[https://www.uniprot.org/uniprot/PUR2_ECOLI PUR2_ECOLI]
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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/1gso_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=1gso ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phosphoribosylamine--glycine ligase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Ealick SE]]
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[[Category: Ealick, S.E.]]
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[[Category: Kappock TJ]]
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[[Category: Kappock, T.J.]]
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[[Category: Stubbe J]]
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[[Category: Stubbe, J.]]
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[[Category: Wang W]]
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[[Category: Wang, W.]]
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[[Category: atp-grasp]]
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[[Category: gar-syn]]
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[[Category: glycinamide ribonucleotide synthetase]]
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[[Category: purine de novo biosynthetic pathway]]
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[[Category: substrate channeling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:16:15 2007''
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Current revision

GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.

PDB ID 1gso

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