1htl: Difference between revisions

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[[Image:1htl.gif|left|200px]]


{{Structure
==MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFORMATIONAL CHANGE: CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN MUTANT VAL 97--> LYS==
|PDB= 1htl |SIZE=350|CAPTION= <scene name='initialview01'>1htl</scene>, resolution 2.5&Aring;
<StructureSection load='1htl' size='340' side='right'caption='[[1htl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1htl]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTL FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htl OCA], [https://pdbe.org/1htl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htl RCSB], [https://www.ebi.ac.uk/pdbsum/1htl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htl ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htl OCA], [http://www.ebi.ac.uk/pdbsum/1htl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1htl RCSB]</span>
[https://www.uniprot.org/uniprot/ELAP_ECOLX ELAP_ECOLX] The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFORMATIONAL CHANGE: CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN MUTANT VAL 97--> LYS'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ht/1htl_consurf.spt"</scriptWhenChecked>
==About this Structure==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
1HTL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTL OCA].  
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==Reference==
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1htl ConSurf].
Mutation of a buried residue causes loss of activity but no conformational change in the heat-labile enterotoxin of Escherichia coli., Merritt EA, Sarfaty S, Pizza M, Domenighini M, Rappuoli R, Hol WG, Nat Struct Biol. 1995 Apr;2(4):269-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7796260 7796260]
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Hol, W G.J.]]
[[Category: Hol WGJ]]
[[Category: Merritt, E A.]]
[[Category: Merritt EA]]
[[Category: enterotoxin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:14 2008''

Latest revision as of 07:26, 23 October 2024

MUTATION OF A BURIED RESIDUE CAUSES LACK OF ACTIVITY BUT NO CONFORMATIONAL CHANGE: CRYSTAL STRUCTURE OF E. COLI HEAT-LABILE ENTEROTOXIN MUTANT VAL 97--> LYS

1htl, resolution 2.50Å

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