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1n67

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|PDB= 1n67 |SIZE=350|CAPTION= <scene name='initialview01'>1n67</scene>, resolution 1.90&Aring;
|PDB= 1n67 |SIZE=350|CAPTION= <scene name='initialview01'>1n67</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1amx|1AMX]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n67 OCA], [http://www.ebi.ac.uk/pdbsum/1n67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n67 RCSB]</span>
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[[Category: Rajashankar, K R.]]
[[Category: Rajashankar, K R.]]
[[Category: Wann, E R.]]
[[Category: Wann, E R.]]
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[[Category: MG]]
 
[[Category: clumping factor]]
[[Category: clumping factor]]
[[Category: dev-igg]]
[[Category: dev-igg]]
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[[Category: staphylococcus aureus]]
[[Category: staphylococcus aureus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:52:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:00 2008''

Revision as of 19:26, 30 March 2008


PDB ID 1n67

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Related: 1AMX


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Clumping Factor A from Staphylococcus aureus


Overview

We report here the crystal structure of the minimal ligand-binding segment of the Staphylococcus aureus MSCRAMM, clumping factor A. This fibrinogen-binding segment contains two similarly folded domains. The fold observed is a new variant of the immunoglobulin motif that we have called DE-variant or the DEv-IgG fold. This subgroup includes the ligand-binding domain of the collagen-binding S.aureus MSCRAMM CNA, and many other structures previously classified as jelly rolls. Structure predictions suggest that the four fibrinogen-binding S.aureus MSCRAMMs identified so far would also contain the same DEv-IgG fold. A systematic docking search using the C-terminal region of the fibrinogen gamma-chain as a probe suggested that a hydrophobic pocket formed between the two DEv-IgG domains of the clumping factor as the ligand-binding site. Mutagenic substitution of residues Tyr256, Pro336, Tyr338 and Lys389 in the clumping factor, which are proposed to contact the terminal residues (408)AGDV(411) of the gamma-chain, resulted in proteins with no or markedly reduced affinity for fibrinogen.

About this Structure

1N67 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A., Deivanayagam CC, Wann ER, Chen W, Carson M, Rajashankar KR, Hook M, Narayana SV, EMBO J. 2002 Dec 16;21(24):6660-72. PMID:12485987

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