4dfr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4dfr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:4dfr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4dfr| PDB=4dfr | SCENE= }}
{{STRUCTURE_4dfr| PDB=4dfr | SCENE= }}
-
'''CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE'''
+
===CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE===
-
==Overview==
+
<!--
-
X-ray data have been extended to 1.7 A for a binary complex of Escherichia coli dihydrofolate reductase with methotrexate and a ternary complex of Lactobacillus casei dihydrofolate reductase with methotrexate and NADPH. Models for both structures have been refined to R factors of 0.15 and include parameters for fixed and liquid solvent. The two species of dihydrofolate reductase resemble one another even more closely than was thought to be the case prior to refinement. Several new structural features have also been discovered. Among them are a cis peptide linking Gly-97 and Gly-98 (L. Casei numbering) in both species, an alpha helix involving residues 43 through 50 in the E. coli enzyme, and the existence of what may be a specific hydration site on exposed alpha helices. Refinement has led to a revised description of the details of methotrexate binding. We now see that a fixed water molecule mediates the interaction between methotrexate's 2-amino group and Thr-116 (L. casei numbering) and that the inhibitor's 4-amino group makes two hydrogen bonds with the enzyme (instead of one). Other revisions are also discussed. A hypothetical model for substrate binding is proposed in which the pteridine ring is turned upside down while all protein and solvent atoms remain fixed. Asp-26 in this model is hydrogen bonded to the substrate's 2-amino group and to N3.
+
The line below this paragraph, {{ABSTRACT_PUBMED_6815178}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 6815178 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_6815178}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Matthews, D A.]]
[[Category: Matthews, D A.]]
[[Category: Oxido-reductase]]
[[Category: Oxido-reductase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:22:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:34:39 2008''

Revision as of 10:34, 3 July 2008

Image:4dfr.png

Template:STRUCTURE 4dfr

CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE

Template:ABSTRACT PUBMED 6815178

About this Structure

4DFR is a Single protein structure of sequence from Escherichia coli b. This structure supersedes the now removed PDB entry 2dfr. Full crystallographic information is available from OCA.

Reference

Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate., Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J, J Biol Chem. 1982 Nov 25;257(22):13650-62. PMID:6815178

Page seeded by OCA on Thu Jul 3 13:34:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4dfr"
Personal tools