1u2p: Difference between revisions

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New page: left|200px<br /><applet load="1u2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u2p, resolution 1.90Å" /> '''Crystal structure of...
 
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[[Image:1u2p.gif|left|200px]]<br /><applet load="1u2p" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1u2p.gif|left|200px]]<br /><applet load="1u2p" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1u2p, resolution 1.90&Aring;" />
caption="1u2p, resolution 1.90&Aring;" />
'''Crystal structure of Mycobacterium tuberculosis Low Molecular Protein Tyrosine Phosphatase (MPtpA) at 1.9A resolution'''<br />
'''Crystal structure of Mycobacterium tuberculosis Low Molecular Protein Tyrosine Phosphatase (MPtpA) at 1.9A resolution'''<br />


==Overview==
==Overview==
The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs, to a distinctive class of phosphotyrosine phosphatases widely distributed, among prokaryotes and eukaryotes. We report here the crystal structure of, LMWPTPase of microbial origin, the first of its kind from Mycobacterium, tuberculosis. The structure was determined to be two crystal forms at 1.9-, and 2.5-A resolutions. These structural forms are compared with those of, the LMWPTPases of eukaryotes. Though the overall structure resembles that, of the eukaryotic LMWPTPases, there are significant changes around the, active site and the protein tyrosine phosphatase (PTP) loop. The variable, loop forming the wall of the crevice leading to the active site is, conformationally unchanged from that of mammalian LMWPTPase; however, differences are observed in the residues involved, suggesting that they, have a role in influencing different substrate specificities. The single, amino acid substitution (Leu12Thr [underlined below]) in the consensus, sequence of the PTP loop, CTGNICRS, has a major role in the stabilization, of the PTP loop, unlike what occurs in mammalian LMWPTPases. A chloride, ion and a glycerol molecule were modeled in the active site where the, chloride ion interacts in a manner similar to that of phosphate with the, main chain nitrogens of the PTP loop. This structural study, in addition, to identifying specific mycobacterial features, may also form the basis, for exploring the mechanism of the substrate specificities of bacterial, LMWPTPases.
The low-molecular-weight protein tyrosine phosphatase (LMWPTPase) belongs to a distinctive class of phosphotyrosine phosphatases widely distributed among prokaryotes and eukaryotes. We report here the crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis. The structure was determined to be two crystal forms at 1.9- and 2.5-A resolutions. These structural forms are compared with those of the LMWPTPases of eukaryotes. Though the overall structure resembles that of the eukaryotic LMWPTPases, there are significant changes around the active site and the protein tyrosine phosphatase (PTP) loop. The variable loop forming the wall of the crevice leading to the active site is conformationally unchanged from that of mammalian LMWPTPase; however, differences are observed in the residues involved, suggesting that they have a role in influencing different substrate specificities. The single amino acid substitution (Leu12Thr [underlined below]) in the consensus sequence of the PTP loop, CTGNICRS, has a major role in the stabilization of the PTP loop, unlike what occurs in mammalian LMWPTPases. A chloride ion and a glycerol molecule were modeled in the active site where the chloride ion interacts in a manner similar to that of phosphate with the main chain nitrogens of the PTP loop. This structural study, in addition to identifying specific mycobacterial features, may also form the basis for exploring the mechanism of the substrate specificities of bacterial LMWPTPases.


==About this Structure==
==About this Structure==
1U2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with CL 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=1U2P OCA].  
1U2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=CL:'>CL</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=1U2P OCA].  


==Reference==
==Reference==
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[[Category: Protein-tyrosine-phosphatase]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Das, A.K.]]
[[Category: Das, A K.]]
[[Category: Madhurantakam, C.]]
[[Category: Madhurantakam, C.]]
[[Category: Mazumdar, P.A.]]
[[Category: Mazumdar, P A.]]
[[Category: Mitra, D.]]
[[Category: Mitra, D.]]
[[Category: Rajakumara, E.]]
[[Category: Rajakumara, E.]]
[[Category: Saha, B.]]
[[Category: Saha, B.]]
[[Category: Sankaranarayanan, R.]]
[[Category: Sankaranarayanan, R.]]
[[Category: Wiker, H.G.]]
[[Category: Wiker, H G.]]
[[Category: CL]]
[[Category: CL]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: tyrosine phosphatase]]
[[Category: tyrosine phosphatase]]


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