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.


1ycl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ycl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ycl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ycl| PDB=1ycl | SCENE= }}
{{STRUCTURE_1ycl| PDB=1ycl | SCENE= }}
-
'''Crystal Structure of B. subtilis LuxS in Complex with a Catalytic 2-Ketone Intermediate'''
+
===Crystal Structure of B. subtilis LuxS in Complex with a Catalytic 2-Ketone Intermediate===
-
==Overview==
+
<!--
-
S-Ribosylhomocysteinase (LuxS) is an Fe(2+)-dependent metalloenzyme that catalyzes the cleavage of the thioether bond in S-ribosylhomocysteine (SRH) to produce homocysteine (Hcys) and 4,5-dihydroxy-2,3-pentanedione (DPD), the precursor of type II bacterial quorum-sensing molecule. The proposed mechanism involves an initial metal-catalyzed aldose-ketose isomerization reaction, which results in the migration of the ribose carbonyl group from its C1 to C2 position and the formation of a 2-ketone intermediate. A repetition of the isomerization reaction shifts the carbonyl group to the C3 position. Subsequent beta-elimination reaction at the C4 and C5 positions completes the catalytic cycle. In this work, a catalytically inactive mutant (C84A) of Co(2+)-substituted Bacillus subtilis LuxS was cocrystallized with the 2-ketone intermediate and the structure was determined to 1.8 A resolution. The structure reveals that the C2 carbonyl oxygen is directly coordinated with the metal ion, providing strong support for the proposed Lewis acid function of the metal ion during catalysis. Cys-84 and Glu-57 are optimally positioned to act as general acids/bases during the isomerization and elimination reactions. In addition, Ser-6, His-11, and Arg-39 are involved in substrate/ intermediate binding through hydrogen bonding interactions. The above conclusions are further confirmed by site-directed mutagenesis and visible absorption spectroscopic studies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15751951}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15751951 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15751951}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Metalloenzyme]]
[[Category: Metalloenzyme]]
[[Category: Quorum sensing]]
[[Category: Quorum sensing]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:09:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:25:19 2008''

Revision as of 05:25, 28 July 2008

Image:1ycl.png

Template:STRUCTURE 1ycl

Crystal Structure of B. subtilis LuxS in Complex with a Catalytic 2-Ketone Intermediate

Template:ABSTRACT PUBMED 15751951

About this Structure

1YCL is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of S-ribosylhomocysteinase (LuxS) in complex with a catalytic 2-ketone intermediate., Rajan R, Zhu J, Hu X, Pei D, Bell CE, Biochemistry. 2005 Mar 15;44(10):3745-53. PMID:15751951

Page seeded by OCA on Mon Jul 28 08:25:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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