1bgi: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1bgi.gif|left|200px]]
[[Image:1bgi.gif|left|200px]]


{{Structure
<!--
|PDB= 1bgi |SIZE=350|CAPTION= <scene name='initialview01'>1bgi</scene>, resolution 1.7&Aring;
The line below this paragraph, containing "STRUCTURE_1bgi", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1bgi| PDB=1bgi  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgi OCA], [http://www.ebi.ac.uk/pdbsum/1bgi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bgi RCSB]</span>
}}


'''ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)'''
'''ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)'''
Line 30: Line 27:
[[Category: Matsuura, Y.]]
[[Category: Matsuura, Y.]]
[[Category: Oki, H.]]
[[Category: Oki, H.]]
[[Category: hydrolase]]
[[Category: Hydrolase]]
[[Category: o-glycosyl]]
[[Category: O-glycosyl]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:28:57 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:00:25 2008''

Revision as of 11:29, 2 May 2008

File:1bgi.gif

Template:STRUCTURE 1bgi

ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE (310K)


OverviewOverview

The structure of orthorhombic hen egg-white lysozyme (HEWL) crystallized at 310 K has been refined at 1.7 A resolution. Large displacements of the side-chain atoms with respect to the tetragonal structure were observed in many places, in contrast to small displacements of the main-chain atoms. A chloride-ion binding site was observed at an interface of two molecules, but at a different position to the binding site in the tetragonal form. The analysis of intermolecular contacts in the crystal has shown the presence of three independent intermolecular contacts which are called macrobonds A, B and C. Arginine side chains are frequently involved in these macrobonds, suggesting that the high frequency of this residue in HEWL may be a possible reason for the multiple polymorphs of this protein. The crystal forms were determined using a light-reflecting device on a four-circle diffractometer. Correlations between crystal forms and the three-dimensional macrobond networks were interpreted in terms of their components in various crystallographic planes, making use of approximate strengths of hydrogen-bond and van der Waals interatomic forces.

About this StructureAbout this Structure

1BGI is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

ReferenceReference

Refined structure of orthorhombic lysozyme crystallized at high temperature: correlation between morphology and intermolecular contacts., Oki H, Matsuura Y, Komatsu H, Chernov AA, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):114-21. Epub 1999, Jan 1. PMID:10089401 Page seeded by OCA on Fri May 2 11:28:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA