2hrv: Difference between revisions

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New page: left|200px<br /><applet load="2hrv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hrv, resolution 1.95Å" /> '''2A CYSTEINE PROTEINA...
 
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[[Image:2hrv.jpg|left|200px]]<br /><applet load="2hrv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2hrv.jpg|left|200px]]<br /><applet load="2hrv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2hrv, resolution 1.95&Aring;" />
caption="2hrv, resolution 1.95&Aring;" />
'''2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2'''<br />
'''2A CYSTEINE PROTEINASE FROM HUMAN RHINOVIRUS 2'''<br />


==Overview==
==Overview==
The crystal structure of the 2A proteinase from human rhinovirus serotype, 2 (HRV2-2A(pro)) has been solved to 1.95 A resolution. The structure has, an unusual, although chymotrypsin-related, fold comprising a unique, four-stranded beta sheet as the N-terminal domain and a six-stranded beta, barrel as the C-terminal domain. A tightly bound zinc ion, essential for, the stability of HRV2-2A(pro), is tetrahedrally coordinated by three, cysteine sulfurs and one histidine nitrogen. The active site consists of a, catalytic triad formed by His18, Asp35 and Cys106. Asp35 is additionally, involved in an extensive hydrogen-bonding network. Modelling studies, reveal a substrate-induced fit that explains the specificity of the, subsites S4, S2, S1 and S1'. The structure of HRV2-2A(pro) suggests the, mechanism of the cis cleavage and its release from the polyprotein.
The crystal structure of the 2A proteinase from human rhinovirus serotype 2 (HRV2-2A(pro)) has been solved to 1.95 A resolution. The structure has an unusual, although chymotrypsin-related, fold comprising a unique four-stranded beta sheet as the N-terminal domain and a six-stranded beta barrel as the C-terminal domain. A tightly bound zinc ion, essential for the stability of HRV2-2A(pro), is tetrahedrally coordinated by three cysteine sulfurs and one histidine nitrogen. The active site consists of a catalytic triad formed by His18, Asp35 and Cys106. Asp35 is additionally involved in an extensive hydrogen-bonding network. Modelling studies reveal a substrate-induced fit that explains the specificity of the subsites S4, S2, S1 and S1'. The structure of HRV2-2A(pro) suggests the mechanism of the cis cleavage and its release from the polyprotein.


==About this Structure==
==About this Structure==
2HRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Picornain_2A Picornain 2A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.29 3.4.22.29] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HRV OCA].  
2HRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Picornain_2A Picornain 2A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.29 3.4.22.29] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRV OCA].  


==Reference==
==Reference==
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[[Category: Picornain 2A]]
[[Category: Picornain 2A]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Cherney, M.M.]]
[[Category: Cherney, M M.]]
[[Category: James, M.N.G.]]
[[Category: James, M N.G.]]
[[Category: Kuechler, E.]]
[[Category: Kuechler, E.]]
[[Category: Liebig, H.D.]]
[[Category: Liebig, H D.]]
[[Category: Petersen, J.F.W.]]
[[Category: Petersen, J F.W.]]
[[Category: Skern, T.]]
[[Category: Skern, T.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: hydrolase (cysteine proteinase)]]
[[Category: hydrolase (cysteine proteinase)]]


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