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1zgg

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[[Image:1zgg.gif|left|200px]]
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[[Image:1zgg.png|left|200px]]
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{{STRUCTURE_1zgg| PDB=1zgg | SCENE= }}
{{STRUCTURE_1zgg| PDB=1zgg | SCENE= }}
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'''Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis'''
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===Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis===
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==Overview==
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The low-molecular-weight (LMW) protein tyrosine phosphatases (PTPs) exist ubiquitously in prokaryotes and eukaryotes and play important roles in cellular processes. We report here the solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis. YwlE consists of a twisted central four-stranded parallel beta-sheet with seven alpha-helices packing on both sides. Similar to LMW PTPs from other organisms, the conformation of the YwlE active site is favorable for phosphotyrosine binding, indicating that it may share a common catalytic mechanism in the hydrolysis of phosphate on tyrosine residue in proteins. Though the overall structure resembles that of the eukaryotic LMW PTPs, significant differences were observed around the active site. Residue Asp115 is likely interacting with residue Arg13 through electrostatic interaction or hydrogen bond interaction to stabilize the conformation of the active cavity, which may be a unique character of bacterial LMW PTPs. Residues in the loop region from Phe40 to Thr48 forming a wall of the active cavity are more flexible than those in other regions. Ala41 and Gly45 are located near the active cavity and form a noncharged surface around it. These unique properties demonstrate that this loop may be involved in interaction with specific substrates. In addition, the results from spin relaxation experiments elucidate further insights into the mobility of the active site. The solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial LMW PTPs.
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The line below this paragraph, {{ABSTRACT_PUBMED_16452434}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16452434 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16452434}}
==About this Structure==
==About this Structure==
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1ZGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGG OCA].
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1ZGG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZGG OCA].
==Reference==
==Reference==
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[[Category: Four-stranded parallel beta sheet]]
[[Category: Four-stranded parallel beta sheet]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:35:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:42:01 2008''

Revision as of 09:42, 29 July 2008

Image:1zgg.png

Template:STRUCTURE 1zgg

Solution structure of a low molecular weight protein tyrosine phosphatase from Bacillus subtilis

Template:ABSTRACT PUBMED 16452434

About this Structure

1ZGG is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.

Reference

Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis., Xu H, Xia B, Jin C, J Bacteriol. 2006 Feb;188(4):1509-17. PMID:16452434

Page seeded by OCA on Tue Jul 29 12:42:01 2008

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