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.


1jog

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jog.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jog.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jog| PDB=1jog | SCENE= }}
{{STRUCTURE_1jog| PDB=1jog | SCENE= }}
-
'''Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase'''
+
===Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase===
-
==Overview==
+
<!--
-
The crystal structure of HI0074 from Haemophilus influenzae, a protein of unknown function, has been determined at a resolution of 2.4 A. The molecules form an up-down, four-helix bundle, and associate into homodimers. The fold is most closely related to the substrate-binding domain of KNTase, yet the amino acid sequences of the two proteins exhibit no significant homology. Sequence analyses of completely and incompletely sequenced genomes reveal that the two adjacent genes, HI0074 and HI0073, and their close relatives comprise a new family of nucleotidyltransferases, with 15 members at the time of writing. The analyses also indicate that this is one of eight families of a large nucleotidyltransferase superfamily, whose members were identified based on the proximity of the nucleotide- and substrate-binding domains on the respective genomes. Both HI0073 and HI0074 were annotated "hypothetical" in the original genome sequencing publication. HI0073 was cloned, expressed, and purified, and was shown to form a complex with HI0074 by polyacrylamide gel electrophoresis under nondenaturing conditions, analytic size exclusion chromatography, and dynamic light scattering. Double- and single-stranded DNA binding assays showed no evidence of DNA binding to HI0074 or to HI0073/HI0074 complex despite the suggestive shape of the putative binding cleft formed by the HI0074 dimer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12486719}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12486719 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12486719}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structure 2 function project]]
[[Category: Structure 2 function project]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:30:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:33:16 2008''

Revision as of 17:33, 1 July 2008

Image:1jog.png

Template:STRUCTURE 1jog

Structure of HI0074 from Heamophilus Influenzae reveals the fold of a substrate binding domain of a nucleotidyltransferase

Template:ABSTRACT PUBMED 12486719

About this Structure

1JOG is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of a new nucleotidyltransferase family: structure, sequence analyses, and solution studies., Lehmann C, Lim K, Chalamasetty VR, Krajewski W, Melamud E, Galkin A, Howard A, Kelman Z, Reddy PT, Murzin AG, Herzberg O, Proteins. 2003 Feb 1;50(2):249-60. PMID:12486719

Page seeded by OCA on Tue Jul 1 20:33:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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