2hm4: Difference between revisions

Revision as of 07:21, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hm4.png

Template:STRUCTURE 2hm4

Nematocyst Outer Wall Antigen, NW1 K21PNematocyst Outer Wall Antigen, NW1 K21P

Template:ABSTRACT PUBMED 17240343

About this StructureAbout this Structure

2HM4 is a Single protein structure of sequence from Hydra vulgaris. Full experimental information is available from OCA.

ReferenceReference

Continuous molecular evolution of protein-domain structures by single amino acid changes., Meier S, Jensen PR, David CN, Chapman J, Holstein TW, Grzesiek S, Ozbek S, Curr Biol. 2007 Jan 23;17(2):173-8. PMID:17240343

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OCA

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 {{STRUCTURE_2hm4|  PDB=2hm4  |  SCENE=  }}
-'''Nematocyst Outer Wall Antigen, NW1 K21P'''
+===Nematocyst Outer Wall Antigen, NW1 K21P===
-==Overview==
+<!--
-Protein structures cluster into families of folds that can result from extremely different amino acid sequences [1]. Because the enormous amount of genetic information generates a limited number of protein folds [2], a particular domain structure often assumes numerous functions. How new protein structures and new functions evolve under these limitations remains elusive. Molecular evolution may be driven by the ability of biomacromolecules to adopt multiple conformations as a bridge between different folds [3-6]. This could allow proteins to explore new structures and new tasks while part of the structural ensemble retains the initial conformation and function as a safeguard [7]. Here we show that a global structural switch can arise from single amino acid changes in cysteine-rich domains (CRD) of cnidarian nematocyst proteins. The ability of these CRDs to form two structures with different disulfide patterns from an identical cysteine pattern is distinctive [8]. By applying a structure-based mutagenesis approach, we demonstrate that a cysteine-rich domain can interconvert between two natively occurring domain structures via a bridge state containing both structures. Comparing cnidarian CRD sequences leads us to believe that the mutations we introduced to stabilize each structure reflect the birth of new protein folds in evolution.
+The line below this paragraph, {{ABSTRACT_PUBMED_17240343}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17240343 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17240343}}
 ==About this Structure==
-HM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HM4 OCA].
+HM4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HM4 OCA].
 ==Reference==
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 [[Category: Evolution]]
 [[Category: Nematocyst]]
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