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.


1noz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1noz.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1noz.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1noz| PDB=1noz | SCENE= }}
{{STRUCTURE_1noz| PDB=1noz | SCENE= }}
-
'''T4 DNA POLYMERASE FRAGMENT (RESIDUES 1-388) AT 110K'''
+
===T4 DNA POLYMERASE FRAGMENT (RESIDUES 1-388) AT 110K===
-
==Overview==
+
<!--
-
We report the crystal structure of an NH2-terminal 388-residue fragment of T4 DNA polymerase (protein N388) refined at 2.2 A resolution. This fragment contains both the 3'-5' exonuclease active site and part of the autologous mRNA binding site (J. D. Karam, personal communication). The structure of a complex between the apoprotein N388 and a substrate, p(dT)3, has been refined at 2.5 A resolution to a crystallographic R-factor of 18.7%. Two divalent metal ion cofactors, Zn(II) and Mn(II), have been located in crystals of protein N388 which had been soaked in solutions containing Zn(II), Mn(II), or both. The structure of the 3'-5' exonuclease domain of protein N388 closely resembles the corresponding region in the Klenow fragment despite minimal sequence identity. The side chains of four carboxylate residues that serve as ligands for the two metal ions required for catalysis are located in geometrically equivalent positions in both proteins with a rms deviation of 0.87 A. There are two main differences between the 3'-5' exonuclease active site regions of the two proteins: (I) the OH of Tyr-497 in the Klenow fragment interacts with the scissile phosphate in the active site whereas the OH of the equivalent tyrosine (Tyr-320) in protein N388 points away from the active center; (II) different residues form of the binding pocket for the 3'-terminal bases of the substrate. In the protein N388 complex the 3'-terminal base of p(dT)3 is rotated approximately 60 degrees relative to the position that the corresponding base occupies in the p(dT)3 complex with the Klenow fragment. Finally, a separate domain (residues 1-96) of protein N388 may be involved in mRNA binding that results in translational regulation of T4 DNA polymerase (Pavlov &amp; Karam, 1994).
+
The line below this paragraph, {{ABSTRACT_PUBMED_8679562}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8679562 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8679562}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Exonuclease]]
[[Category: Exonuclease]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:47:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:09:34 2008''

Revision as of 17:09, 28 July 2008

Image:1noz.png

Template:STRUCTURE 1noz

T4 DNA POLYMERASE FRAGMENT (RESIDUES 1-388) AT 110K

Template:ABSTRACT PUBMED 8679562

About this Structure

1NOZ is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Crystal structures of an NH2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions., Wang J, Yu P, Lin TC, Konigsberg WH, Steitz TA, Biochemistry. 1996 Jun 25;35(25):8110-9. PMID:8679562

Page seeded by OCA on Mon Jul 28 20:09:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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