2a1d
From Proteopedia
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| - | [[Image:2a1d.gif|left|200px]] | + | [[Image:2a1d.gif|left|200px]] |
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| - | '''Staphylocoagulase bound to bovine thrombin''' | + | {{Structure |
| + | |PDB= 2a1d |SIZE=350|CAPTION= <scene name='initialview01'>2a1d</scene>, resolution 3.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Staphylocoagulase bound to bovine thrombin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A1D is a [ | + | 2A1D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1D OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation., Friedrich R, Panizzi P, Kawabata S, Bode W, Bock PE, Fuentes-Prior P, J Biol Chem. 2006 Jan 13;281(2):1188-95. Epub 2005 Oct 17. PMID:[http:// | + | Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation., Friedrich R, Panizzi P, Kawabata S, Bode W, Bock PE, Fuentes-Prior P, J Biol Chem. 2006 Jan 13;281(2):1188-95. Epub 2005 Oct 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16230338 16230338] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: prothrombin activator]] | [[Category: prothrombin activator]] | ||
| - | ''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 15:44:11 2008'' |
Revision as of 13:44, 20 March 2008
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| , resolution 3.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Thrombin, with EC number 3.4.21.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Staphylocoagulase bound to bovine thrombin
Overview
Staphylocoagulase (SC) is a protein secreted by the human pathogen, Staphylococcus aureus, that activates human prothrombin (ProT) by inducing a conformational change. SC-bound ProT efficiently clots fibrinogen, thus bypassing the physiological blood coagulation pathway. The crystal structure of a fully active SC fragment, SC-(1-325), bound to human prethrombin 2 showed that the SC-(1-325) N terminus inserts into the Ile(16) pocket of prethrombin 2, thereby inducing expression of a functional catalytic site in the cognate zymogen without peptide bond cleavage. As shown here, SC-(1-325) binds to bovine and human ProT with similar affinity but activates the bovine zymogen only very poorly. By contrast to the approximately 2-fold difference in chromogenic substrate kinetic constants between human thrombin and the SC-(1-325).human (pro)thrombin complexes, SC-(1-325).bovine ProT shows a 3,500-fold lower k(cat)/K(m) compared with free bovine thrombin, because of a 47-fold increase in K(m) and a 67-fold decrease in k(cat). The SC-(1-325).bovine ProT complex is approximately 5,800-fold less active compared with its human counterpart. Comparison of human and bovine fibrinogen as substrates of human and bovine thrombin and the SC-(1-325).(pro)thrombin complexes indicates that the species specificity of SC-(1-325) cofactor activity is determined primarily by differences in conformational activation of bound ProT. These results suggest that the catalytic site in the SC-(1-325).bovine ProT complex is incompletely formed. The current crystal structure of SC-(1-325).bovine thrombin reveals that SC would dock similarly to the bovine proenzyme, whereas the bovine (pro)thrombin-characteristic residues Arg(144) and Arg(145) would likely interfere with insertion of the SC N terminus, thus explaining the greatly reduced activation of bovine ProT.
About this Structure
2A1D is a Protein complex structure of sequences from Bos taurus and Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation., Friedrich R, Panizzi P, Kawabata S, Bode W, Bock PE, Fuentes-Prior P, J Biol Chem. 2006 Jan 13;281(2):1188-95. Epub 2005 Oct 17. PMID:16230338
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