1inp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1inp.jpg|left|200px]]<br /><applet load="1inp" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1inp.jpg|left|200px]]
-
caption="1inp, resolution 2.3&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION'''<br />
+
{{Structure
 +
|PDB= 1inp |SIZE=350|CAPTION= <scene name='initialview01'>1inp</scene>, resolution 2.3&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
 +
|ACTIVITY= [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]
 +
|GENE= BOVINE BRAIN CDNA=20 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF INOSITOL POLYPHOSPHATE 1-PHOSPHATASE AT 2.3 ANGSTROMS RESOLUTION'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1INP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INP OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7947723 7947723]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/7947723 7947723]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Inositol-1,4-bisphosphate 1-phosphatase]]
[[Category: Inositol-1,4-bisphosphate 1-phosphatase]]
Line 22: Line 31:
[[Category: hydrolase(phosphoric monoester)]]
[[Category: hydrolase(phosphoric monoester)]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:39 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:52:38 2008''

Revision as of 09:52, 20 March 2008


PDB ID 1inp

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands:
Gene: BOVINE BRAIN CDNA=20 (Bos taurus)
Activity: Inositol-1,4-bisphosphate 1-phosphatase, with EC number 3.1.3.57
Coordinates: save as pdb, mmCIF, xml



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. 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 Thu Mar 20 11:52:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools