147l

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|PDB= 147l |SIZE=350|CAPTION= <scene name='initialview01'>147l</scene>, resolution 2.00&Aring;
|PDB= 147l |SIZE=350|CAPTION= <scene name='initialview01'>147l</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
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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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|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]
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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>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=147l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=147l OCA], [http://www.ebi.ac.uk/pdbsum/147l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=147l RCSB]</span>
}}
}}
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==About this Structure==
==About this Structure==
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147L 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=147L OCA].
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147L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=147L 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://www.ncbi.nlm.nih.gov/pubmed/8259514 8259514]
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]
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[[Category: Enterobacteria phage t2]]
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[[Category: Enterobacteria phage t4]]
[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baldwin, E.]]
[[Category: Baldwin, E.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
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[[Category: BME]]
 
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[[Category: CL]]
 
[[Category: hydrolase(o-glycosyl)]]
[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:49:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:28:20 2008''

Revision as of 15:28, 30 March 2008


PDB ID 147l

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: ,
Activity: Lysozyme, with EC number 3.2.1.17
Resources: FirstGlance, OCA, PDBsum, RCSB
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

147L 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

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