143l
From Proteopedia
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| - | [[Image:143l.gif|left|200px]] | + | [[Image:143l.gif|left|200px]] |
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| - | '''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME''' | + | {{Structure |
| + | |PDB= 143l |SIZE=350|CAPTION= <scene name='initialview01'>143l</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ROLE OF BACKBONE FLEXIBILITY IN THE ACCOMMODATION OF VARIANTS THAT REPACK THE CORE OF T4 LYSOZYME''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 143L is a [ | + | 143L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t2 Enterobacteria phage t2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=143L OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8259514 8259514] |
[[Category: Enterobacteria phage t2]] | [[Category: Enterobacteria phage t2]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: hydrolase(o-glycosyl)]] | [[Category: hydrolase(o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:49:29 2008'' |
Revision as of 07:49, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 t2. 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
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