1i2v: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1i2v.jpg|left|200px]]
{{Seed}}
[[Image:1i2v.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i2v|  PDB=1i2v  |  SCENE=  }}  
{{STRUCTURE_1i2v|  PDB=1i2v  |  SCENE=  }}  


'''NMR SOLUTION STRUCTURES OF AN ANTIFUNGAL AND ANTIBACTERIAL MUTANT OF HELIOMICIN'''
===NMR SOLUTION STRUCTURES OF AN ANTIFUNGAL AND ANTIBACTERIAL MUTANT OF HELIOMICIN===




==Overview==
<!--
In response to an experimental infection, the lepidopteran Heliothis virescens produces an antifungal protein named heliomicin. Heliomicin displays sequence similarities with antifungal plant defensins and antibacterial or antifungal insect defensins. To gain information about the structural elements required for either antifungal or antibacterial activity, heliomicin and selected point-mutated variants were expressed in yeast as fusion proteins. The effects of mutations, defined by comparing the primary structure of heliomicin with the sequences of members of the insect defensin family, were analyzed using antibacterial and antifungal assays. One of the variants shows significant activity against Gram-positive bacteria while remaining efficient against fungi. The three-dimensional structures of this variant and of the wild-type protein were determined by two-dimensional (1)H NMR to establish a correlation between structure and antibacterial or antifungal activity. Wild-type and mutated heliomicins adopt a similar scaffold, including the so-called cysteine-stabilized alphabeta motif. A comparison of their structures with other defensin-type molecules indicates that common hydrophobic characteristics can be assigned to all the antifungal proteins. A comparative analysis of various structural features of heliomicin mutant and of antibacterial defensins enables common properties to be assessed, which will help to design new mutants with increased antibacterial activity.
The line below this paragraph, {{ABSTRACT_PUBMED_11580275}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11580275 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11580275}}


==About this Structure==
==About this Structure==
1I2V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2V OCA].  
1I2V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I2V OCA].  


==Reference==
==Reference==
Line 30: Line 34:
[[Category: Vovelle, F.]]
[[Category: Vovelle, F.]]
[[Category: Alpha-beta protein]]
[[Category: Alpha-beta protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:30:22 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:19:41 2008''

Revision as of 07:19, 1 July 2008

File:1i2v.png

Template:STRUCTURE 1i2v

NMR SOLUTION STRUCTURES OF AN ANTIFUNGAL AND ANTIBACTERIAL MUTANT OF HELIOMICIN

Template:ABSTRACT PUBMED 11580275

About this Structure

1I2V is a Single protein structure of sequence from Heliothis virescens. Full experimental information is available from OCA.

Reference

Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities., Lamberty M, Caille A, Landon C, Tassin-Moindrot S, Hetru C, Bulet P, Vovelle F, Biochemistry. 2001 Oct 9;40(40):11995-2003. PMID:11580275

Page seeded by OCA on Tue Jul 1 10:19:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1i2v&oldid=609895"