1nf2: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1nf2.gif|left|200px]]
{{Seed}}
[[Image:1nf2.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nf2|  PDB=1nf2  |  SCENE=  }}  
{{STRUCTURE_1nf2|  PDB=1nf2  |  SCENE=  }}  


'''X-ray crystal structure of TM0651 from Thermotoga maritima'''
===X-ray crystal structure of TM0651 from Thermotoga maritima===




==Overview==
<!--
We have determined the crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima, TM0651 (gi 4981173), at 2.2 A resolution by selenomethionine single-wavelength anomalous diffraction (SAD) techniques. TM0651 is a member of the haloacid dehalogenase (HAD) superfamily, with sequence homology to trehalose-6-phosphate phosphatase and sucrose-6(F)-phosphate phosphohydrolase. Selenomethionine labeled TM0651 crystallized in space group C2 with three monomers per asymmetric unit. Each monomer has approximate dimensions of 65 x 40 x 35 A(3), and contains two domains: a domain of known hydrolase fold characteristic of the HAD family, and a domain with a new tertiary fold consisting of a six-stranded beta-sheet surrounded by four alpha-helices. There is one disulfide bond between residues Cys35 and Cys265 in each monomer. One magnesium ion and one sulfate ion are bound in the active site. The superposition of active site residues with other HAD family members indicates that TM0651 is very likely a phosphatase that acts through the formation of a phosphoaspartate intermediate, which is supported by both NMR titration data and a biochemical assay. Structural and functional database searches and the presence of many aromatic residues in the interface of the two domains suggest the substrate of TM0651 is a carbohydrate molecule. From the crystal structure and NMR data, the protein likely undergoes a conformational change upon substrate binding.
The line below this paragraph, {{ABSTRACT_PUBMED_12824492}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12824492 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12824492}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Structural proteomic]]
[[Category: Structural proteomic]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:27:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:47:41 2008''

Revision as of 00:47, 29 July 2008

File:1nf2.png

Template:STRUCTURE 1nf2

X-ray crystal structure of TM0651 from Thermotoga maritima

Template:ABSTRACT PUBMED 12824492

About this Structure

1NF2 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima., Shin DH, Roberts A, Jancarik J, Yokota H, Kim R, Wemmer DE, Kim SH, Protein Sci. 2003 Jul;12(7):1464-72. PMID:12824492

Page seeded by OCA on Tue Jul 29 03:47:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1nf2&oldid=725728"