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.

2av5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2av5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2av5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2av5| PDB=2av5 | SCENE= }}
{{STRUCTURE_2av5| PDB=2av5 | SCENE= }}
-
'''Crystal structure of Pyrococcus furiosus Pop5, an archaeal Ribonuclease P protein'''
+
===Crystal structure of Pyrococcus furiosus Pop5, an archaeal Ribonuclease P protein===
-
==Overview==
+
<!--
-
We have used NMR spectroscopy and x-ray crystallography to determine the three-dimensional structure of PF1378 (Pfu Pop5), one of four protein subunits of archaeal RNase P that shares a homolog in the eukaryotic enzyme. RNase P is an essential and ubiquitous ribonucleoprotein enzyme required for maturation of tRNA. In bacteria, the enzyme's RNA subunit is responsible for cleaving the single-stranded 5' leader sequence of precursor tRNA molecules (pre-tRNA), whereas the protein subunit assists in substrate binding. Although in bacteria the RNase P holoenzyme consists of one large catalytic RNA and one small protein subunit, in archaea and eukarya the enzyme contains several (&gt; or =4) protein subunits, each of which lacks sequence similarity to the bacterial protein. The functional role of the proteins is poorly understood, as is the increased complexity in comparison to the bacterial enzyme. Pfu Pop5 has been directly implicated in catalysis by the observation that it pairs with PF1914 (Pfu Rpp30) to functionally reconstitute the catalytic domain of the RNA subunit. The protein adopts an alpha-beta sandwich fold highly homologous to the single-stranded RNA binding RRM domain. Furthermore, the three-dimensional arrangement of Pfu Pop5's structural elements is remarkably similar to that of the bacterial protein subunit. NMR spectra have been used to map the interaction of Pop5 with Pfu Rpp30. The data presented permit tantalizing hypotheses regarding the role of this protein subunit shared by archaeal and eukaryotic RNase P.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16418270}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16418270 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16418270}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Wilson, R C.]]
[[Category: Wilson, R C.]]
[[Category: Ribonuclease p]]
[[Category: Ribonuclease p]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:30:46 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:31:03 2008''

Revision as of 05:31, 28 July 2008

Image:2av5.png

Template:STRUCTURE 2av5

Crystal structure of Pyrococcus furiosus Pop5, an archaeal Ribonuclease P protein

Template:ABSTRACT PUBMED 16418270

About this Structure

2AV5 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Structure of Pfu Pop5, an archaeal RNase P protein., Wilson RC, Bohlen CJ, Foster MP, Bell CE, Proc Natl Acad Sci U S A. 2006 Jan 24;103(4):873-8. Epub 2006 Jan 17. PMID:16418270

Page seeded by OCA on Mon Jul 28 08:31:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2av5"
Personal tools