1inp
From Proteopedia
(New page: 200px<br /><applet load="1inp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1inp, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1inp.jpg|left|200px]]<br /><applet load="1inp" size=" | + | [[Image:1inp.jpg|left|200px]]<br /><applet load="1inp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1inp, resolution 2.3Å" /> | caption="1inp, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bovine inositol polyphosphate 1-phosphatase (1-ptase), M(r) = 44,000, is a | + | Bovine inositol polyphosphate 1-phosphatase (1-ptase), M(r) = 44,000, is a Mg(2+)-dependent/Li(+)-sensitive enzyme that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. We have determined the crystal structure of recombinant bovine 1-ptase in the presence of Mg2+ by multiple isomorphous replacement. The structure is currently refined to an R value of 0.198 for 15,563 reflections within a resolution range of 8.0-2.3 A. 1-Ptase is monomeric in the crystal, consistent with biochemical data, and folds into an alternatively layered alpha/beta/alpha/beta sandwich. The central core of 1-ptase consists of a six-stranded antiparallel beta sheet perpendicular to two parallel three-turn alpha-helices. The beta sheet is flanked by two antiparallel six-turn alpha-helices aligned parallel to the beta sheet, and the central helices are flanked by a five-stranded largely parallel beta sheet. Two neighboring metal binding sites are located in adjacent acidic pockets formed by the intersection of several secondary structure elements including an unusual kink structure formed by the "DPIDST" sequence motif. The fold of 1-ptase is similar to that of two other metal-dependent/Li(+)-sensitive phosphatases, inositol monophosphate phosphatase and fructose 1,6-bisphosphatase despite minimal amino acid identity. Comparison of the active-site pockets of these proteins will likely provide insight into substrate binding and the mechanisms of metal-dependent catalysis and Li+ inhibition. |
==About this Structure== | ==About this Structure== | ||
| - | 1INP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-1,4-bisphosphate_1-phosphatase Inositol-1,4-bisphosphate 1-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.57 3.1.3.57] Full crystallographic information is available from [http:// | + | 1INP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-1,4-bisphosphate_1-phosphatase Inositol-1,4-bisphosphate 1-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.57 3.1.3.57] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, Z.]] | [[Category: Chen, Z.]] | ||
| - | [[Category: Majerus, P | + | [[Category: Majerus, P W.]] |
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
| - | [[Category: Ponder, J | + | [[Category: Ponder, J W.]] |
| - | [[Category: York, J | + | [[Category: York, J D.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: hydrolase(phosphoric monoester)]] | [[Category: hydrolase(phosphoric monoester)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:39 2008'' |
Revision as of 11:13, 21 February 2008
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CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION
Overview
Bovine inositol polyphosphate 1-phosphatase (1-ptase), M(r) = 44,000, is a Mg(2+)-dependent/Li(+)-sensitive enzyme that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. We have determined the crystal structure of recombinant bovine 1-ptase in the presence of Mg2+ by multiple isomorphous replacement. The structure is currently refined to an R value of 0.198 for 15,563 reflections within a resolution range of 8.0-2.3 A. 1-Ptase is monomeric in the crystal, consistent with biochemical data, and folds into an alternatively layered alpha/beta/alpha/beta sandwich. The central core of 1-ptase consists of a six-stranded antiparallel beta sheet perpendicular to two parallel three-turn alpha-helices. The beta sheet is flanked by two antiparallel six-turn alpha-helices aligned parallel to the beta sheet, and the central helices are flanked by a five-stranded largely parallel beta sheet. Two neighboring metal binding sites are located in adjacent acidic pockets formed by the intersection of several secondary structure elements including an unusual kink structure formed by the "DPIDST" sequence motif. The fold of 1-ptase is similar to that of two other metal-dependent/Li(+)-sensitive phosphatases, inositol monophosphate phosphatase and fructose 1,6-bisphosphatase despite minimal amino acid identity. Comparison of the active-site pockets of these proteins will likely provide insight into substrate binding and the mechanisms of metal-dependent catalysis and Li+ inhibition.
About this Structure
1INP is a Single protein structure of sequence from Bos taurus with as ligand. Active as Inositol-1,4-bisphosphate 1-phosphatase, with EC number 3.1.3.57 Full crystallographic information is available from OCA.
Reference
Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution., York JD, Ponder JW, Chen ZW, Mathews FS, Majerus PW, Biochemistry. 1994 Nov 15;33(45):13164-71. PMID:7947723
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