We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1lrp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lrp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lrp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lrp| PDB=1lrp | SCENE= }}
{{STRUCTURE_1lrp| PDB=1lrp | SCENE= }}
-
'''COMPARISON OF THE STRUCTURES OF CRO AND LAMBDA REPRESSOR PROTEINS FROM BACTERIOPHAGE LAMBDA'''
+
===COMPARISON OF THE STRUCTURES OF CRO AND LAMBDA REPRESSOR PROTEINS FROM BACTERIOPHAGE LAMBDA===
-
==Overview==
+
<!--
-
The three-dimensional structures of cro repressor protein and of the amino-terminal domain of lambda repressor protein, both from bacteriophage lambda, are compared. The second and third alpha-helices, alpha 2 and alpha 3, are shown to have essentially identical conformations in the two proteins, confirming the significance of the amino acid sequence homology previously noted between these and other DNA binding proteins in the region corresponding to these helices. The correspondence between the two-helical units in cro and lambda repressor protein is better than the striking agreement noted previously between two-helical units in cro and catabolite gene-activator protein. Parts of the first alpha-helices of repressor and cro show a structural correspondence that suggests a revised sequence homology between the two proteins in their extreme amino-terminal regions. In particular, there is a short loop between the alpha 1 and alpha 2 helices of lambda repressor that is missing from cro. This structural difference may account for the observed differences found with different cros and repressors in the pattern of phosphates whose ethylation prevents the binding of these proteins to their specific recognition sites. Although the two proteins have strikingly similar alpha 2-alpha 3 helical units that are presumed to bind to DNA in an essentially similar manner, stereochemical restrictions prevent the alpha 2-alpha 3 units of the respective proteins aligning on the DNA in exactly the same way.
+
The line below this paragraph, {{ABSTRACT_PUBMED_6226802}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 6226802 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_6226802}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Pabo, C.]]
[[Category: Pabo, C.]]
[[Category: Dna binding regulatory protein]]
[[Category: Dna binding regulatory protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:13:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:54:18 2008''

Revision as of 18:54, 2 July 2008

Image:1lrp.png

Template:STRUCTURE 1lrp

COMPARISON OF THE STRUCTURES OF CRO AND LAMBDA REPRESSOR PROTEINS FROM BACTERIOPHAGE LAMBDA

Template:ABSTRACT PUBMED 6226802

About this Structure

1LRP is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

Comparison of the structures of cro and lambda repressor proteins from bacteriophage lambda., Ohlendorf DH, Anderson WF, Lewis M, Pabo CO, Matthews BW, J Mol Biol. 1983 Sep 25;169(3):757-69. PMID:6226802

Page seeded by OCA on Wed Jul 2 21:54:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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