1k92

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1k92" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k92, resolution 1.60&Aring;" /> '''Crystal Structure of...)
Current revision (07:45, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1k92.gif|left|200px]]<br /><applet load="1k92" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1k92, resolution 1.60&Aring;" />
 
-
'''Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase'''<br />
 
-
==Overview==
+
==Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase==
-
BACKGROUND: Argininosuccinate synthetase (AS) is the rate-limiting enzyme, of both the urea and arginine-citrulline cycles. In mammals, deficiency of, AS leads to citrullinemia, a debilitating and often fatal autosomal, recessive urea cycle disorder, whereas its overexpression for sustained, nitric oxide production via the arginine-citrulline cycle leads to the, potentially fatal hypotension associated with septic and cytokine-induced, circulatory shock. RESULTS: The crystal structure of E. coli AS (EAS) has, been determined by the use of selenomethionine incorporation and MAD, phasing. The structure has been refined at 1.6 A resolution in the absence, of its substrates and at 2.0 A in the presence of aspartate and citrulline, (EAS*CIT+ASP). Each monomer of this tetrameric protein has two structural, domains: a nucleotide binding domain similar to that of the "N-type" ATP, pyrophosphatase class of enzymes, and a novel catalytic/multimerization, domain. The EAS*CIT+ASP structure clearly describes the binding of, citrulline at the cleft between the two domains and of aspartate to a loop, of the nucleotide binding domain, whereas homology modeling with the, N-type ATP pyrophosphatases has provided the location of ATP binding., CONCLUSIONS: The first three-dimensional structures of AS are reported., The fold of the nucleotide binding domain confirms AS as the fourth, structurally defined member of the N-type ATP pyrophosphatases. The, structures identify catalytically important residues and suggest the, requirement for a conformational change during the catalytic cycle., Sequence similarity between the bacterial and human enzymes has been used, for providing insight into the structural and functional effects of, observed clinical mutations.
+
<StructureSection load='1k92' size='340' side='right'caption='[[1k92]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1k92]] 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=1K92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K92 FirstGlance]. <br>
-
1K92 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 SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Argininosuccinate_synthase Argininosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.5 6.3.4.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K92 OCA].
+
</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>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k92 OCA], [https://pdbe.org/1k92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k92 RCSB], [https://www.ebi.ac.uk/pdbsum/1k92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k92 ProSAT]</span></td></tr>
-
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis., Lemke CT, Howell PL, Structure. 2001 Dec;9(12):1153-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11738042 11738042]
+
</table>
-
[[Category: Argininosuccinate synthase]]
+
== Function ==
 +
[https://www.uniprot.org/uniprot/ASSY_ECOLI ASSY_ECOLI]
 +
== 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/k9/1k92_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=1k92 ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Howell, P.L.]]
+
[[Category: Howell PL]]
-
[[Category: Lemke, C.T.]]
+
[[Category: Lemke CT]]
-
[[Category: GOL]]
+
-
[[Category: SO4]]
+
-
[[Category: n-type atp pyrophosphatase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:58:06 2007''
+

Current revision

Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase

PDB ID 1k92

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k92"
Personal tools