This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1sjd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1sjd.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1sjd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sjd| PDB=1sjd | SCENE= }}
{{STRUCTURE_1sjd| PDB=1sjd | SCENE= }}
-
'''x-ray structure of o-succinylbenzoate synthase complexed with n-succinyl phenylglycine'''
+
===x-ray structure of o-succinylbenzoate synthase complexed with n-succinyl phenylglycine===
-
==Overview==
+
<!--
-
Divergent evolution of enzyme function is commonly explained by a gene duplication event followed by mutational changes that allow the protein encoded by the copy to acquire a new function. An alternate hypothesis is that this process is facilitated when the progenitor enzyme acquires a second function while maintaining the original activity. This phenomenon has been suggested to occur in the o-succinylbenzoate synthase (OSBS) from a species of Amycolatopsis that catalyzes not only the physiological syn-dehydration reaction of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate but also an accidental racemization of N-acylamino acids [Palmer, D. R., Garrett, J. B., Sharma, V., Meganathan, R., Babbitt, P. C., and Gerlt, J. A. (1999) Biochemistry 38, 4252-4258]. To understand the molecular basis of this promiscuity, three-dimensional structures of liganded complexes of this enzyme have been determined, including the product of the OSBS reaction and three N-acylamino acid substrates for the N-acylamino acid racemase (NAAAR) reaction, N-acetylmethionine, N-succinylmethionine, and N-succinylphenylglycine, to 2.2, 2.3, 2.1, and 1.9 A resolution, respectively. These structures show how the active-site cavity can accommodate both the hydrophobic substrate for the OSBS reaction and the substrates for the accidental NAAAR reaction. As expected, the N-acylamino acid is sandwiched between lysines 163 and 263, which function as the catalytic bases for the abstraction of the alpha-proton in the (R)- and (S)-racemization reactions, respectively [Taylor Ringia, E. A., Garrett, J. B, Thoden, J. B., Holden, H. M., Rayment, I., and Gerlt, J. A. (2004) Biochemistry 42, 224-229]. Importantly, the protein forms specific favorable interactions with the hydrophobic amino acid side chain, alpha-carbon, carboxylate, and the polar components of the N-acyl linkage. Accommodation of the components of the N-acyl linkage appears to be the reason that this enzyme is capable of a racemization reaction on these substrates, whereas the orthologous OSBS from Escherichia coli lacks this functionality.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15134446}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15134446 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15134446}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Thoden, J B.]]
[[Category: Thoden, J B.]]
[[Category: Racemase]]
[[Category: Racemase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:46:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:27:27 2008''

Revision as of 22:27, 27 July 2008

Image:1sjd.png

Template:STRUCTURE 1sjd

x-ray structure of o-succinylbenzoate synthase complexed with n-succinyl phenylglycine

Template:ABSTRACT PUBMED 15134446

About this Structure

1SJD is a Single protein structure of sequence from Amycolatopsis sp.. Full crystallographic information is available from OCA.

Reference

Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis., Thoden JB, Taylor Ringia EA, Garrett JB, Gerlt JA, Holden HM, Rayment I, Biochemistry. 2004 May 18;43(19):5716-27. PMID:15134446

Page seeded by OCA on Mon Jul 28 01:27:27 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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