1hon

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(New page: 200px<br /><applet load="1hon" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hon, resolution 2.3&Aring;" /> '''STRUCTURE OF GUANINE ...)
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[[Image:1hon.gif|left|200px]]<br /><applet load="1hon" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hon, resolution 2.3&Aring;" />
 
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'''STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI AT PH 6.5 AND 25 DEGREE CELSIUS'''<br />
 
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==Overview==
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==STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI AT PH 6.5 AND 25 DEGREE CELSIUS==
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Structures of adenylosuccinate synthetase from Escherichia coli complexed, with guanosine-5'-(beta,gamma-imido) triphosphate and, guanosine-5'-(beta,gamma-methylene)triphosphate in the presence and the, absence of Mg2+ have been refined to R-factors below 0.2 against data to a, nominal resolution of 2.7 A. Asp333 of the synthetase hydrogen bonds to, the exocyclic 2-amino and endocyclic N1 groups of the guanine nucleotide, base, whereas the hydroxyl of Ser414 and the backbone amide of Lys331, hydrogen bond to the 6-oxo position. The side chains of Lys331 and Pro417, pack against opposite faces of the guanine nucleotide base. The synthetase, recognizes neither the N7 position of guanine nucleotides nor the ribose, group. Electron density for the guanine-5'-(beta,gamma-imido) triphosphate, complex is consistent with a mixture of the triphosphate nucleoside and, its hydrolyzed diphosphate nucleoside bound to the active site. The base, ribose, and alpha-phosphate positions overlap, but the beta-phosphates, occupy different binding sites. The binding of, guanosine-5'-(beta,gamma-methylene)triphosphate to the active site is, comparable with that of guanosine-5'-(beta, gamma-imido)triphosphate. No, electron density, however, for the corresponding diphosphate nucleoside is, observed. In addition, electron density for bound Mg2+ is absent in these, nucleotide complexes. The guanine nucleotide complexes of the synthetase, are compared with complexes of other GTP-binding proteins and to a, preliminary structure of the complex of GDP, IMP, Mg2+, and succinate with, the synthetase. The enzyme, under conditions reported here, does not, undergo a conformational change in response to the binding of guanine, nucleotides, and minimally IMP and/or Mg2+ must be present in order to, facilitate the complete recognition of the guanine nucleotide by the, synthetase.
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<StructureSection load='1hon' size='340' side='right'caption='[[1hon]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hon]] is a 2 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=1HON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HON 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]] 2.3&#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=GNH:AMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNH</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=1hon FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hon OCA], [https://pdbe.org/1hon PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hon RCSB], [https://www.ebi.ac.uk/pdbsum/1hon PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hon ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PURA_ECOLI PURA_ECOLI] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011]
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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/ho/1hon_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=1hon 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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1HON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GNH as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HON OCA].
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*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli., Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1996 Jun 28;271(26):15407-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8663109 8663109]
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[[Category: Adenylosuccinate synthase]]
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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: Bruns, C.]]
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[[Category: Bruns C]]
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[[Category: Fromm, H.J.]]
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[[Category: Fromm HJ]]
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[[Category: Honzatko, R.B.]]
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[[Category: Honzatko RB]]
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[[Category: Hou, Z.]]
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[[Category: Hou Z]]
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[[Category: Poland, B.W.]]
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[[Category: Poland BW]]
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[[Category: GNH]]
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[[Category: gtp-binding enzymes]]
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[[Category: ligase]]
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[[Category: purine nucleotide biosynthesis]]
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[[Category: synthetase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:42:45 2007''
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Current revision

STRUCTURE OF GUANINE NUCLEOTIDE (GPPCP) COMPLEX OF ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI AT PH 6.5 AND 25 DEGREE CELSIUS

PDB ID 1hon

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