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.


1hqk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hqk.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1hqk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hqk| PDB=1hqk | SCENE= }}
{{STRUCTURE_1hqk| PDB=1hqk | SCENE= }}
-
'''CRYSTAL STRUCTURE ANALYSIS OF LUMAZINE SYNTHASE FROM AQUIFEX AEOLICUS'''
+
===CRYSTAL STRUCTURE ANALYSIS OF LUMAZINE SYNTHASE FROM AQUIFEX AEOLICUS===
-
==Overview==
+
<!--
-
An open reading frame optimized for expression of 6,7-dimethyl-8-ribityl-lumazine synthase of the hyperthermophilic bacterium Aquifex aeolicus in Escherichia coli was synthesized and expressed in a recombinant E. coli strain to a level of around 15 %. The recombinant protein was purified by heat-treatment and gel-filtration. The protein was crystallized in the cubic space group I23 with the cell dimensions a = b = c = 180.8 A, and diffraction data were collected to 1.6 A resolution. The structure was solved by molecular replacement using lumazine synthase from Bacillus subtilis as search model. The structure of the A. aeolicus enzyme was refined to a resolution of 1.6 A. The spherical protein consists of 60 identical subunits with strict icosahedral 532 symmetry. The subunit fold is closely related to that of the B. subtilis enzyme (rmsd 0.80 A). The extremely thermostable lumazine synthase from A. aeolicus has a melting temperature of 119.9 degrees C. Compared to other icosahedral and pentameric lumazine synthases, the A. aeolicus enzyme has the largest accessible surface presented by charged residues and the smallest surface presented by hydrophobic residues. It also has the largest number of ion-pairs per subunit. Two ion-pair networks involving two, respectively three, stacking arginine residues assume a distinct role in linking adjacent subunits. The findings indicate the influence of the optimization of hydrophobic and ionic contacts in gaining thermostability.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11237620}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11237620 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11237620}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Vitamin biosynthesis]]
[[Category: Vitamin biosynthesis]]
[[Category: X-ray structure analysis]]
[[Category: X-ray structure analysis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:07:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:32:43 2008''

Revision as of 05:32, 1 July 2008

Image:1hqk.png

Template:STRUCTURE 1hqk

CRYSTAL STRUCTURE ANALYSIS OF LUMAZINE SYNTHASE FROM AQUIFEX AEOLICUS

Template:ABSTRACT PUBMED 11237620

About this Structure

1HQK is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons., Zhang X, Meining W, Fischer M, Bacher A, Ladenstein R, J Mol Biol. 2001 Mar 9;306(5):1099-114. PMID:11237620

Page seeded by OCA on Tue Jul 1 08:32:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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