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.


1i4n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i4n.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1i4n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i4n| PDB=1i4n | SCENE= }}
{{STRUCTURE_1i4n| PDB=1i4n | SCENE= }}
-
'''CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA'''
+
===CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA===
-
==Overview==
+
<!--
-
The crystal structure of the thermostable indoleglycerol-phosphate synthase from Thermotoga maritima (tIGPS) was determined at 2.5 A resolution. It was compared with the structures of the thermostable sIGPS from Sulfolobus solfataricus and of the thermolabile eIGPS from Escherichia coli. The main chains of the three (beta alpha)(8)-barrel proteins superimpose closely, and the packing of side chains in the beta-barrel cores, as well as the architecture of surface loops, is very similar. Both thermostable proteins have, however, 17 strong salt bridges, compared with only 10 in eIGPS. The number of additional salt bridges in tIGPS and sIGPS correlates well with their reduced rate of irreversible thermal inactivation at 90 degrees C. Only 3 of 17 salt bridges in tIGPS and sIGPS are topologically conserved. The major difference between the two proteins is the preference for interhelical salt bridges in sIGPS and intrahelical ones in tIGPS. The different implementation of salt bridges in the closely related proteins suggests that the stabilizing effect of salt bridges depends rather on the sum of their individual contributions than on their location. This observation is consistent with a protein unfolding mechanism where the simultaneous breakdown of all salt bridges is the rate-determining step.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11741953}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11741953 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11741953}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Thermostable tim-barrel protein]]
[[Category: Thermostable tim-barrel protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:34:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:24:37 2008''

Revision as of 07:24, 1 July 2008

Image:1i4n.png

Template:STRUCTURE 1i4n

CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA

Template:ABSTRACT PUBMED 11741953

About this Structure

1I4N is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges., Knochel T, Pappenberger A, Jansonius JN, Kirschner K, J Biol Chem. 2002 Mar 8;277(10):8626-34. Epub 2001 Dec 10. PMID:11741953

Page seeded by OCA on Tue Jul 1 10:24:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i4n"
Personal tools