1wrm: Difference between revisions

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New page: left|200px<br /> <applet load="1wrm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wrm, resolution 1.50Å" /> '''Crystal structure o...
 
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[[Image:1wrm.gif|left|200px]]<br />
[[Image:1wrm.gif|left|200px]]<br /><applet load="1wrm" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1wrm" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1wrm, resolution 1.50&Aring;" />
caption="1wrm, resolution 1.50&Aring;" />
'''Crystal structure of JSP-1'''<br />
'''Crystal structure of JSP-1'''<br />


==Overview==
==Overview==
Human JNK stimulatory phosphatase-1 (JSP-1) is a novel member of dual, specificity phosphatases. A C-terminus truncated JSP-1 was expressed in, Escherichia coli and was crystallized using the sitting-drop vapor, diffusion method. Thin-plate crystals obtained at 278 K belong to a, monoclinic space group, C2, with unit-cell parameters a = 84.0 A, b = 49.3, A, c = 47.3 A, and beta = 119.5 degrees , and diffract up to 1.5 A, resolution at 100 K. The structure of JSP-1 has a single compact, (alpha/beta) domain, which consists of six alpha-helices and five, beta-strands, and shows a conserved structural scaffold in regard to both, DSPs and PTPs. A cleft formed by a PTP-loop at the active site is very, shallow, and is occupied by one sulfonate compound, MES, at the bottom. In, the binary complex structure of JSP-1 with MES, the conformations of three, important segments in regard to the catalytic mechanism are not similar to, those in PTP1B. JSP-1 has no loop corresponding to the Lys120-loop of, PTP1B, and tryptophan residue corresponding to the substrate-stacking in, PTP1B is substituted by alanine residue in JSP-1.
Human JNK stimulatory phosphatase-1 (JSP-1) is a novel member of dual specificity phosphatases. A C-terminus truncated JSP-1 was expressed in Escherichia coli and was crystallized using the sitting-drop vapor diffusion method. Thin-plate crystals obtained at 278 K belong to a monoclinic space group, C2, with unit-cell parameters a = 84.0 A, b = 49.3 A, c = 47.3 A, and beta = 119.5 degrees , and diffract up to 1.5 A resolution at 100 K. The structure of JSP-1 has a single compact (alpha/beta) domain, which consists of six alpha-helices and five beta-strands, and shows a conserved structural scaffold in regard to both DSPs and PTPs. A cleft formed by a PTP-loop at the active site is very shallow, and is occupied by one sulfonate compound, MES, at the bottom. In the binary complex structure of JSP-1 with MES, the conformations of three important segments in regard to the catalytic mechanism are not similar to those in PTP1B. JSP-1 has no loop corresponding to the Lys120-loop of PTP1B, and tryptophan residue corresponding to the substrate-stacking in PTP1B is substituted by alanine residue in JSP-1.


==About this Structure==
==About this Structure==
1WRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WRM OCA].  
1WRM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WRM OCA].  


==Reference==
==Reference==
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[[Category: phosphatase]]
[[Category: phosphatase]]


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