We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1iw8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1iw8.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1iw8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1iw8| PDB=1iw8 | SCENE= }}
{{STRUCTURE_1iw8| PDB=1iw8 | SCENE= }}
-
'''Crystal Structure of a mutant of acid phosphatase from Escherichia blattae (G74D/I153T)'''
+
===Crystal Structure of a mutant of acid phosphatase from Escherichia blattae (G74D/I153T)===
-
==Overview==
+
<!--
-
Escherichia blattae non-specific acid phosphatase (EB-NSAP) possesses a pyrophosphate-nucleoside phosphotransferase activity, which is C-5'-position selective. Current mutational and structural data were used to generate a mutant EB-NSAP for a potential industrial application as an effective and economical protein catalyst in synthesizing nucleotides from nucleosides. First, Gly74 and Ile153 were replaced by Asp and Thr, respectively, since the corresponding replacements in the homologous enzyme from Morganella morganii reduced the K(m) value for inosine and thus increased the productivity of 5'-IMP. We determined the crystal structure of G74D/I153T, which has a reduced K(m) value for inosine, as expected. The tertiary structure of G74D/I153T was virtually identical to that of the wild-type. In addition, neither of the introduced side chains of Asp74 and Thr153 is directly involved in the interaction with inosine in a hypothetical binding mode of inosine to EB-NSAP, although both residues are situated near a potential inosine-binding site. These findings suggested that a slight structural change caused by an amino acid replacement around the potential inosine-binding site could significantly reduce the K(m) value. Prompted by this hypothesis, we designed several mutations and introduced them to G74D/I153T, to decrease the K(m) value further. This strategy produced a S72F/G74D/I153T mutant with a 5.4-fold lower K(m) value and a 2.7-fold higher V(max) value as compared to the wild-type EB-NSAP.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12200535}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12200535 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12200535}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Suzuki, E.]]
[[Category: Suzuki, E.]]
[[Category: All alpha]]
[[Category: All alpha]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:29:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:06:41 2008''

Revision as of 11:06, 1 July 2008

Image:1iw8.png

Template:STRUCTURE 1iw8

Crystal Structure of a mutant of acid phosphatase from Escherichia blattae (G74D/I153T)

Template:ABSTRACT PUBMED 12200535

About this Structure

1IW8 is a Single protein structure of sequence from Escherichia blattae. Full crystallographic information is available from OCA.

Reference

Enhancement of nucleoside phosphorylation activity in an acid phosphatase., Ishikawa K, Mihara Y, Shimba N, Ohtsu N, Kawasaki H, Suzuki E, Asano Y, Protein Eng. 2002 Jul;15(7):539-43. PMID:12200535

Page seeded by OCA on Tue Jul 1 14:06:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iw8"
Personal tools