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.


1ktu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ktu.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1ktu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ktu| PDB=1ktu | SCENE= }}
{{STRUCTURE_1ktu| PDB=1ktu | SCENE= }}
-
'''NuiA'''
+
===NuiA===
-
==Overview==
+
<!--
-
Nuclease A (NucA) from Anabaena sp. is a non-specific endonuclease able to degrade single and double-stranded DNA and RNA. The endonucleolytic activity is inhibited by the nuclease A inhibitor (NuiA), which binds to NucA with 1:1 stoichiometry and picomolar affinity. In order to better understand the mechanism of inhibition, the solution structure of NuiA was determined by NMR methods. The fold of NuiA is an alpha-beta-alpha sandwich but standard database searches by DALI and TOP revealed no structural homologies. A visual inspection of alpha-beta-alpha folds in the CATH database revealed similarities to the PR-1-like fold (SCOP nomenclature). The similarities include the ordering of secondary structural elements, a single helix on one face of the alpha-beta-alpha sandwich, and three helices on the other face. However, a major difference is in the IV helix, which in the PR-1 fold is short and perpendicular to the I and III helices, but in NuiA is long and parallel to the I and III helices. Additionally, a strand insertion in the beta-sheet makes the NuiA beta-sheet completely antiparallel in organization. The fast time-scale motions of NuiA, characterized by enhanced flexibility of the extended loop between helices III and IV, also show similarities to P14a, which is a PR-1 fold. We propose that the purpose of the PR-1 fold is to form a stable scaffold to present this extended structure for biological interactions with other proteins. This hypothesis is supported by data that show that when NuiA is bound to NucA significant changes in chemical shift occur in the extended loop between helices III and IV.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12095254}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12095254 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12095254}}
==About this Structure==
==About this Structure==
-
1KTU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTU OCA].
+
1KTU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTU OCA].
==Reference==
==Reference==
Line 35: Line 39:
[[Category: Nuia]]
[[Category: Nuia]]
[[Category: Pr-1-like]]
[[Category: Pr-1-like]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:09:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:59:34 2008''

Revision as of 07:59, 2 July 2008

Image:1ktu.png

Template:STRUCTURE 1ktu

NuiA

Template:ABSTRACT PUBMED 12095254

About this Structure

1KTU is a Single protein structure of sequence from Anabaena sp.. Full experimental information is available from OCA.

Reference

The nuclease A inhibitor represents a new variation of the rare PR-1 fold., Kirby TW, Mueller GA, DeRose EF, Lebetkin MS, Meiss G, Pingoud A, London RE, J Mol Biol. 2002 Jul 19;320(4):771-82. PMID:12095254

Page seeded by OCA on Wed Jul 2 10:59:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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