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[[Image:1nht.gif|left|200px]]<br />
<applet load="1nht" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nht, resolution 2.5&Aring;" />
'''ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K'''<br />


==Overview==
==ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K==
Crystal structures of adenylosuccinate synthetase from Escherichia coli, complexed with Mg2+, 6-thiophosphoryl-IMP, GDP, and hadacidin at 298 and, 100 K have been refined to R-factors of 0.171 and 0.206 against data to, 2.8 and 2.5 A resolution, respectively. Interactions of GDP, Mg2+ and, hadacidin are similar to those observed for the same ligands in the, complex of IMP, GDP, NO3-, Mg2+ and hadacidin (Poland, B. W., Fromm, H. J., &amp; Honzatko, R. B. (1996). J. Mol. Biol. 264, 1013-1027). Although crystals, were grown from solutions containing 6-mercapto-IMP and GTP, the electron, density at the active site is consistent with 6-thiophosphoryl-IMP and, GDP. Asp-13 and Gln-224 probably work in concert to stabilize the, 6-thioanion of 6-mercapto-IMP, which in turn is the nucleophile in the, displacement of GDP from the gamma-phosphate of GTP. Once formed, 6-thiophosphoryl-IMP is stable in the active site of the enzyme under the, conditions of the structural investigation. The direct observation of, 6-thiophosphoryl-IMP in the active site is consistent with the putative, generation of 6-phosphoryl-IMP along the reaction pathway of the, synthetase.
<StructureSection load='1nht' size='340' side='right'caption='[[1nht]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nht]] 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=1NHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NHT FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGS:2-DEAZO-6-THIOPHOSPHATE+GUANOSINE-5-MONOPHOSPHATE'>PGS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nht OCA], [https://pdbe.org/1nht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nht RCSB], [https://www.ebi.ac.uk/pdbsum/1nht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nht ProSAT]</span></td></tr>
</table>
== Function ==
[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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nh/1nht_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1nht ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NHT 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 MG, GDP, HAD and PGS as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Structure known Active Sites: ASP, GNS and IMP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NHT OCA].
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli., Poland BW, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1997 Jun 13;272(24):15200-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9182542 9182542]
[[Category: Adenylosuccinate synthase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bruns, C.A.]]
[[Category: Bruns CA]]
[[Category: Fromm, H.J.]]
[[Category: Fromm HJ]]
[[Category: Honzatko, R.B.]]
[[Category: Honzatko RB]]
[[Category: Poland, B.W.]]
[[Category: Poland BW]]
[[Category: GDP]]
[[Category: HAD]]
[[Category: MG]]
[[Category: PGS]]
[[Category: gtp-hydrolysing enzymes]]
[[Category: ligase]]
[[Category: purine nucleotide biosynthesis]]
[[Category: synthetase]]
[[Category: x-ray crystallography]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:58:55 2007''

Latest revision as of 10:56, 14 February 2024

ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100KENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K

Structural highlights

1nht is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1nht, resolution 2.50Å

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