2in0: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,596 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,596 edits
No edit summary
Line 1: Line 1:
[[Image:2in0.gif|left|200px]]
{{Seed}}
[[Image:2in0.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2in0|  PDB=2in0  |  SCENE=  }}  
{{STRUCTURE_2in0|  PDB=2in0  |  SCENE=  }}  


'''crystal structure of Mtu recA intein splicing domain'''
===crystal structure of Mtu recA intein splicing domain===




==Overview==
<!--
The 440 amino acid Mtu recA intein consists of independent protein-splicing and endonuclease domains. Previously, removal of the central endonuclease domain of the intein, and selection for function, generated a 168 residue mini-intein, DeltaI-SM, that had splicing activity similar to that of the full-length, wild-type protein. A D422G mutation (DeltaI-CM) increased C-terminal cleavage activity. Using the DeltaI-SM mini-intein structure (presented here) as a guide, we previously generated a highly active 139 residue mini-intein, DeltaDeltaI(hh)-SM, by replacing 36 amino acid residues in the residual endonuclease loop with a seven-residue beta-turn from the autoprocessing domain of Hedgehog protein. The three-dimensional structures of DeltaI-SM, DeltaDeltaI(hh)-SM, and two variants, DeltaDeltaI(hh)-CM and DeltaDeltaI(hh), have been determined to evaluate the effects of the minimization on intein integrity and to investigate the structural and functional consequences of the D422G mutation. These structural studies show that Asp422 is capable of interacting with both the N and C termini. These interactions are lacking in the CM variant, but are replaced by contacts with water molecules. Accordingly, additional mutagenesis of residue 422, combined with mutations that isolate N-terminal and C-terminal cleavage, showed that the side-chain of Asp422 plays a role in both N and C-terminal cleavage, thereby suggesting that this highly conserved residue regulates the balance between the two reactions.
The line below this paragraph, {{ABSTRACT_PUBMED_17254599}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17254599 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17254599}}


==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Roey, P Van.]]
[[Category: Roey, P Van.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:40:32 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:48:49 2008''

Revision as of 21:49, 27 July 2008

File:2in0.png

Template:STRUCTURE 2in0

crystal structure of Mtu recA intein splicing domain

Template:ABSTRACT PUBMED 17254599

About this Structure

2IN0 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue., Van Roey P, Pereira B, Li Z, Hiraga K, Belfort M, Derbyshire V, J Mol Biol. 2007 Mar 16;367(1):162-73. Epub 2006 Dec 23. PMID:17254599

Page seeded by OCA on Mon Jul 28 00:48:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2in0&oldid=674291"