1azz
From Proteopedia
(New page: 200px<br /><applet load="1azz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1azz, resolution 2.3Å" /> '''FIDDLER CRAB COLLAGEN...) |
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| - | [[Image:1azz.gif|left|200px]]<br /><applet load="1azz" size=" | + | [[Image:1azz.gif|left|200px]]<br /><applet load="1azz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1azz, resolution 2.3Å" /> | caption="1azz, resolution 2.3Å" /> | ||
'''FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN'''<br /> | '''FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of fiddler crab collagenase complexed with the | + | The crystal structure of fiddler crab collagenase complexed with the dimeric serine protease inhibitor ecotin at 2.5 A resolution reveals an extended cleft providing binding sites for at least 11 contiguous substrate residues. Comparison of the positions of nine intermolecular main chain hydrogen bonding interactions in the cleft, with the known sequences at the cleavage site of type I collagen, suggests that the protease binding loop of ecotin adopts a conformation mimicking that of the cleaved strand of collagen. A well-defined groove extending across the binding surface of the enzyme readily accommodates the two other polypeptide chains of the triple-helical substrate. These observations permit construction of a detailed molecular model for collagen recognition and cleavage by this invertebrate serine protease. Ecotin undergoes a pronounced internal structural rearrangement which permits binding in the observed conformation. The capacity for such rearrangement appears to be a key determinant of its ability to inhibit a wide range of serine proteases. |
==About this Structure== | ==About this Structure== | ||
| - | 1AZZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Celuca_pugilator Celuca pugilator] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Brachyurin Brachyurin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.32 3.4.21.32] Full crystallographic information is available from [http:// | + | 1AZZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Celuca_pugilator Celuca pugilator] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Brachyurin Brachyurin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.32 3.4.21.32] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AZZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fletterick, R | + | [[Category: Fletterick, R J.]] |
| - | [[Category: Perona, J | + | [[Category: Perona, J J.]] |
[[Category: collagen]] | [[Category: collagen]] | ||
[[Category: complex]] | [[Category: complex]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:03 2008'' |
Revision as of 09:50, 21 February 2008
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FIDDLER CRAB COLLAGENASE COMPLEXED TO ECOTIN
Overview
The crystal structure of fiddler crab collagenase complexed with the dimeric serine protease inhibitor ecotin at 2.5 A resolution reveals an extended cleft providing binding sites for at least 11 contiguous substrate residues. Comparison of the positions of nine intermolecular main chain hydrogen bonding interactions in the cleft, with the known sequences at the cleavage site of type I collagen, suggests that the protease binding loop of ecotin adopts a conformation mimicking that of the cleaved strand of collagen. A well-defined groove extending across the binding surface of the enzyme readily accommodates the two other polypeptide chains of the triple-helical substrate. These observations permit construction of a detailed molecular model for collagen recognition and cleavage by this invertebrate serine protease. Ecotin undergoes a pronounced internal structural rearrangement which permits binding in the observed conformation. The capacity for such rearrangement appears to be a key determinant of its ability to inhibit a wide range of serine proteases.
About this Structure
1AZZ is a Protein complex structure of sequences from Celuca pugilator and Escherichia coli. Active as Brachyurin, with EC number 3.4.21.32 Full crystallographic information is available from OCA.
Reference
Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix., Perona JJ, Tsu CA, Craik CS, Fletterick RJ, Biochemistry. 1997 May 6;36(18):5381-92. PMID:9154920
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