1egr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1egr.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1egr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1egr| PDB=1egr | SCENE= }}
{{STRUCTURE_1egr| PDB=1egr | SCENE= }}
-
'''SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN'''
+
===SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN===
-
==Overview==
+
<!--
-
The determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed as the input for the structure calculations, for which the distance geometry program DIANA was used followed by simulated annealing with the program X-PLOR. The molecular architecture of reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1942053}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1942053 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1942053}}
==About this Structure==
==About this Structure==
-
1EGR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGR OCA].
+
1EGR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGR OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Xia, T H.]]
[[Category: Xia, T H.]]
[[Category: Electron transport]]
[[Category: Electron transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:04:56 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:40:26 2008''

Revision as of 21:40, 30 June 2008

Template:STRUCTURE 1egr

SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN

Template:ABSTRACT PUBMED 1942053

About this Structure

1EGR is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin., Sodano P, Xia TH, Bushweller JH, Bjornberg O, Holmgren A, Billeter M, Wuthrich K, J Mol Biol. 1991 Oct 20;221(4):1311-24. PMID:1942053

Page seeded by OCA on Tue Jul 1 00:40:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools