143l

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[[Image:143l.gif|left|200px]]
[[Image:143l.gif|left|200px]]
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{{Structure
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|PDB= 143l |SIZE=350|CAPTION= <scene name='initialview01'>143l</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_143l", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span>
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{{STRUCTURE_143l| PDB=143l | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=143l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=143l OCA], [http://www.ebi.ac.uk/pdbsum/143l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=143l RCSB]</span>
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'''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME'''
'''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME'''
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[[Category: Baldwin, E.]]
[[Category: Baldwin, E.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:30:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:00 2008''
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Revision as of 06:30, 2 May 2008

Image:143l.gif

Template:STRUCTURE 143l

ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME


Overview

To understand better how the packing of side chains within the core influences protein structure and stability, the crystal structures were determined for eight variants of T4 lysozyme, each of which contains three to five substitutions at adjacent interior sites. Concerted main-chain and side-chain displacements, with movements of helical segments as large as 0.8 angstrom, were observed. In contrast, the angular conformations of the mutated side chains tended to remain unchanged, with torsion angles within 20 degrees of those in the wild-type structure. These observations suggest that not only the rotation of side chains but also movements of the main chain must be considered in the evaluation of which amino acid sequences are compatible with a given protein fold.

About this Structure

143L is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme., Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW, Science. 1993 Dec 10;262(5140):1715-8. PMID:8259514 Page seeded by OCA on Fri May 2 09:30:02 2008

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