1cxu: Difference between revisions

New page: left|200px<br /><applet load="1cxu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cxu, resolution 1.42Å" /> '''1.42A RESOLUTION ASV...
 
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[[Image:1cxu.gif|left|200px]]<br /><applet load="1cxu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1cxu.gif|left|200px]]<br /><applet load="1cxu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1cxu, resolution 1.42&Aring;" />
caption="1cxu, resolution 1.42&Aring;" />
'''1.42A RESOLUTION ASV INTEGRASE CORE DOMAIN FROM CITRATE'''<br />
'''1.42A RESOLUTION ASV INTEGRASE CORE DOMAIN FROM CITRATE'''<br />


==Overview==
==Overview==
Six crystal structures of the core domain of integrase (IN) from avian, sarcoma virus (ASV) and its active-site derivative containing an Asp64 --&gt;, Asn substitution have been solved at atomic resolution ranging 1.02-1.42, A. The high-quality data provide new structural information about the, active site of the enzyme and clarify previous inconsistencies in the, description of this fragment. The very high resolution of the data and, excellent quality of the refined models explain the dynamic properties of, IN and the multiple conformations of its disordered residues. They also, allow an accurate description of the solvent structure and help to locate, other molecules bound to the enzyme. A detailed analysis of the flexible, active-site region, in particular the loop formed by residues 144-154, suggests conformational changes which may be associated with substrate, binding and enzymatic activity. The pH-dependent conformational changes of, the active-site loop correlates with the pH vs activity profile observed, for ASV IN.
Six crystal structures of the core domain of integrase (IN) from avian sarcoma virus (ASV) and its active-site derivative containing an Asp64 --&gt; Asn substitution have been solved at atomic resolution ranging 1.02-1.42 A. The high-quality data provide new structural information about the active site of the enzyme and clarify previous inconsistencies in the description of this fragment. The very high resolution of the data and excellent quality of the refined models explain the dynamic properties of IN and the multiple conformations of its disordered residues. They also allow an accurate description of the solvent structure and help to locate other molecules bound to the enzyme. A detailed analysis of the flexible active-site region, in particular the loop formed by residues 144-154, suggests conformational changes which may be associated with substrate binding and enzymatic activity. The pH-dependent conformational changes of the active-site loop correlates with the pH vs activity profile observed for ASV IN.


==About this Structure==
==About this Structure==
1CXU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus] with CIT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CXU OCA].  
1CXU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Avian_sarcoma_virus Avian sarcoma virus] with <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CXU OCA].  


==Reference==
==Reference==
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[[Category: mixed beta-sheet surrounded by alpha-helices]]
[[Category: mixed beta-sheet surrounded by alpha-helices]]


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