From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1inp.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1inp.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1inp| PDB=1inp | SCENE= }} | | {{STRUCTURE_1inp| PDB=1inp | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7947723}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7947723 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_7947723}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Ponder, J W.]] | | [[Category: Ponder, J W.]] |
| | [[Category: York, J D.]] | | [[Category: York, J D.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:11:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:37:27 2008'' |
Revision as of 10:37, 1 July 2008
Template:STRUCTURE 1inp
CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 7947723
About this Structure
1INP is a Single protein structure of sequence from Bos taurus. 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
Page seeded by OCA on Tue Jul 1 13:37:27 2008
