1elx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1elx.gif|left|200px]]<br /><applet load="1elx" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1elx.gif|left|200px]]
-
caption="1elx, resolution 2.6&Aring;" />
+
 
-
'''E. COLI ALKALINE PHOSPHATASE MUTANT (S102A)'''<br />
+
{{Structure
 +
|PDB= 1elx |SIZE=350|CAPTION= <scene name='initialview01'>1elx</scene>, resolution 2.6&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1]
 +
|GENE= PHOA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
 +
}}
 +
 
 +
'''E. COLI ALKALINE PHOSPHATASE MUTANT (S102A)'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1ELX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkaline_phosphatase Alkaline phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.1 3.1.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELX OCA].
+
1ELX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELX OCA].
==Reference==
==Reference==
-
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102., Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER, J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9533886 9533886]
+
Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102., Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER, J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9533886 9533886]
[[Category: Alkaline phosphatase]]
[[Category: Alkaline phosphatase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 25: Line 34:
[[Category: hydrolase]]
[[Category: hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:10 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:22 2008''

Revision as of 08:57, 20 March 2008

Image:1elx.gif


PDB ID 1elx

Drag the structure with the mouse to rotate
, resolution 2.6Å
Ligands: , and
Gene: PHOA (Escherichia coli)
Activity: Alkaline phosphatase, with EC number 3.1.3.1
Coordinates: save as pdb, mmCIF, xml



E. COLI ALKALINE PHOSPHATASE MUTANT (S102A)


Overview

Escherichia coli alkaline phosphatase (EC 3.1.3.1) is a non-specific phosphomonoesterase that catalyzes the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol. We investigated the nature of the primary nucleophile, fulfilled by the deprotonated Ser102, in the catalytic mechanism by mutating this residue to glycine, alanine and cysteine. The efficiencies of the S102G, S102A and S102C enzymes were 6 x 10(5)-fold, 10(5)-fold and 10(4)-fold lower than the wild-type enzyme, respectively, as measured by the kcat/Km ratio, still substantially higher than the non-catalyzed reaction. In order to investigate the structural details of the altered active site, the enzymes were crystallized and their structures determined. The enzymes crystallized in a new crystal form corresponding to the space group P6322. Each structure has phosphate at each active site and shows little departure from the wild-type model. For the S102G and S102A enzymes, the phosphate occupies the same position as in the wild-type enzyme, while in the S102C enzyme it is displaced by 2.5 A. This kinetic and structural study suggests an explanation for differences in catalytic efficiency of the mutant enzymes and provides a means to study the nature and strength of different nucleophiles in the same environment. The analysis of these results provides insight into the mechanisms of other classes of phosphatases that do not utilize a serine nucleophile.

About this Structure

1ELX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102., Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER, J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:9533886

Page seeded by OCA on Thu Mar 20 10:57:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1elx"
Personal tools