1nqj: Difference between revisions
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[[Image:1nqj.jpg|left|200px]] | [[Image:1nqj.jpg|left|200px]] | ||
'''CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.0 ANGSTROM RESOLUTION IN ABSENCE OF CALCIUM''' | {{Structure | ||
|PDB= 1nqj |SIZE=350|CAPTION= <scene name='initialview01'>1nqj</scene>, resolution 1.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=LI:LITHIUM ION'>LI</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Microbial_collagenase Microbial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.3 3.4.24.3] | |||
|GENE= ColG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1498 Clostridium histolyticum]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.0 ANGSTROM RESOLUTION IN ABSENCE OF CALCIUM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NQJ is a [ | 1NQJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_histolyticum Clostridium histolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQJ OCA]. | ||
==Reference== | ==Reference== | ||
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation., Wilson JJ, Matsushita O, Okabe A, Sakon J, EMBO J. 2003 Apr 15;22(8):1743-52. PMID:[http:// | A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation., Wilson JJ, Matsushita O, Okabe A, Sakon J, EMBO J. 2003 Apr 15;22(8):1743-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12682007 12682007] | ||
[[Category: Clostridium histolyticum]] | [[Category: Clostridium histolyticum]] | ||
[[Category: Microbial collagenase]] | [[Category: Microbial collagenase]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
''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 13:00:28 2008'' | ||
Revision as of 14:00, 20 March 2008
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| , resolution 1.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | ColG (Clostridium histolyticum) | ||||||
| Activity: | Microbial collagenase, with EC number 3.4.24.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CLOSTRIDIUM HISTOLYTICUM COLG COLLAGENASE COLLAGEN-BINDING DOMAIN 3B AT 1.0 ANGSTROM RESOLUTION IN ABSENCE OF CALCIUM
OverviewOverview
The crystal structure of a collagen-binding domain (CBD) with an N-terminal domain linker from Clostridium histolyticum class I collagenase was determined at 1.00 A resolution in the absence of calcium (1NQJ) and at 1.65 A resolution in the presence of calcium (1NQD). The mature enzyme is composed of four domains: a metalloprotease domain, a spacing domain and two CBDs. A 12-residue-long linker is found at the N-terminus of each CBD. In the absence of calcium, the CBD reveals a beta-sheet sandwich fold with the linker adopting an alpha-helix. The addition of calcium unwinds the linker and anchors it to the distal side of the sandwich as a new beta-strand. The conformational change of the linker upon calcium binding is confirmed by changes in the Stokes and hydrodynamic radii as measured by size exclusion chromatography and by dynamic light scattering with and without calcium. Furthermore, extensive mutagenesis of conserved surface residues and collagen-binding studies allow us to identify the collagen-binding surface of the protein and propose likely collagen-protein binding models.
About this StructureAbout this Structure
1NQJ is a Single protein structure of sequence from Clostridium histolyticum. Full crystallographic information is available from OCA.
ReferenceReference
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation., Wilson JJ, Matsushita O, Okabe A, Sakon J, EMBO J. 2003 Apr 15;22(8):1743-52. PMID:12682007
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