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.


1wxx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wxx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1wxx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wxx| PDB=1wxx | SCENE= }}
{{STRUCTURE_1wxx| PDB=1wxx | SCENE= }}
-
'''Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8'''
+
===Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8===
-
==Overview==
+
<!--
-
The Thermus thermophilus hypothetical protein TTHA1280 belongs to a family of predicted S-adenosyl-L-methionine (AdoMet) dependent RNA methyltransferases (MTases) present in many bacterial and archaeal species. Inspection of amino-acid sequence motifs common to class I Rossmann-fold-like MTases suggested a specific role as an RNA 5-methyluridine MTase. Selenomethionine (SeMet) labelled and native versions of the protein were expressed, purified and crystallized. Two crystal forms of the SeMet-labelled apoprotein were obtained: SeMet-ApoI and SeMet-ApoII. Cocrystallization of the native protein with S-adenosyl-L-homocysteine (AdoHcy) yielded a third crystal form, Native-AdoHcy. The SeMet-ApoI structure was solved by the multiple anomalous dispersion method and refined at 2.55 A resolution. The SeMet-ApoII and Native-AdoHcy structures were solved by molecular replacement and refined at 1.80 and 2.60 A, respectively. TTHA1280 formed a homodimer in the crystals and in solution. Each subunit folds into a three-domain structure composed of a small N-terminal PUA domain, a central alpha/beta-domain and a C-terminal Rossmann-fold-like MTase domain. The three domains form an overall clamp-like shape, with the putative active site facing a deep cleft. The architecture of the active site is consistent with specific recognition of uridine and catalysis of methyl transfer to the 5-carbon position. The cleft is suitable in size and charge distribution for binding single-stranded RNA.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16511182}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16511182 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16511182}}
==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Thermus thermophillus]]
[[Category: Thermus thermophillus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:17:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:44:43 2008''

Revision as of 04:44, 28 July 2008

Template:STRUCTURE 1wxx

Crystal structure of Tt1595, a putative SAM-dependent methyltransferase from Thermus thermophillus HB8

Template:ABSTRACT PUBMED 16511182

About this Structure

1WXX is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structures of a putative RNA 5-methyluridine methyltransferase, Thermus thermophilus TTHA1280, and its complex with S-adenosyl-L-homocysteine., Pioszak AA, Murayama K, Nakagawa N, Ebihara A, Kuramitsu S, Shirouzu M, Yokoyama S, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Oct 1;61(Pt, 10):867-74. Epub 2005 Sep 30. PMID:16511182

Page seeded by OCA on Mon Jul 28 07:44:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools