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.


1mbz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mbz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mbz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mbz| PDB=1mbz | SCENE= }}
{{STRUCTURE_1mbz| PDB=1mbz | SCENE= }}
-
'''BETA-LACTAM SYNTHETASE WITH TRAPPED INTERMEDIATE'''
+
===BETA-LACTAM SYNTHETASE WITH TRAPPED INTERMEDIATE===
-
==Overview==
+
<!--
-
The catalytic cycle of the ATP/Mg(2+)-dependent enzyme beta-lactam synthetase (beta-LS) from Streptomyces clavuligerus has been observed through a series of x-ray crystallographic snapshots. Chemistry is initiated by the ordered binding of ATP/Mg(2+) and N(2)-(carboxyethyl)-l-arginine (CEA) to the apoenzyme. The apo and ATP/Mg(2+) structures described here, along with the previously described CEA.alpha,beta-methyleneadenosine 5'-triphosphate (CEA.AMP-CPP)/Mg(2+) structure, illuminate changes in active site geometry that favor adenylation. In addition, an acyladenylate intermediate has been trapped. The substrate analog N(2)-(carboxymethyl)-l-arginine (CMA) was adenylated by ATP in the crystal and represents a close structural analog of the previously proposed CEA-adenylate intermediate. Finally, the structure of the ternary product complex deoxyguanidinoproclavaminic acid (DGPC).AMP/PP(i)/Mg(2+) has been determined. The CMA-AMP/PP(i)/Mg(2+) and DGPC.AMP/PP(i)/Mg(2+) structures reveal interactions in the active site that facilitate beta-lactam formation. All of the ATP-bound structures differ from the previously described CEA.AMP-CPP/Mg(2+) structure in that two Mg(2+) ions are found in the active sites. These Mg(2+) ions play critical roles in both the adenylation and beta-lactamization reactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12409610}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12409610 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12409610}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Clavulanic acid]]
[[Category: Clavulanic acid]]
[[Category: Deoxyguanidinoproclavaminic acid]]
[[Category: Deoxyguanidinoproclavaminic acid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:52:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:39:00 2008''

Revision as of 20:39, 2 July 2008

Template:STRUCTURE 1mbz

BETA-LACTAM SYNTHETASE WITH TRAPPED INTERMEDIATE

Template:ABSTRACT PUBMED 12409610

About this Structure

1MBZ is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.

Reference

The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots., Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC, Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14752-7. Epub 2002 Oct 30. PMID:12409610

Page seeded by OCA on Wed Jul 2 23:39:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools