1hfc
From Proteopedia
(New page: 200px<br /> <applet load="1hfc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hfc, resolution 1.5Å" /> '''1.56 ANGSTROM STRUCT...) |
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| - | [[Image:1hfc.gif|left|200px]]<br /> | + | [[Image:1hfc.gif|left|200px]]<br /><applet load="1hfc" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hfc" size=" | + | |
caption="1hfc, resolution 1.5Å" /> | caption="1hfc, resolution 1.5Å" /> | ||
'''1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE'''<br /> | '''1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of a 19 kDa active fragment of human | + | The X-ray crystal structure of a 19 kDa active fragment of human fibroblast collagenase has been determined by the multiple isomorphous replacement method and refined at 1.56 A resolution to an R-factor of 17.4%. The current structure includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two zincs and a calcium). The overall topology of the enzyme, comprised of a five stranded beta-sheet and three alpha-helices, is similar to the thermolysin-like metalloproteinases. There are some important differences between the collagenase and thermolysin families of enzymes. The active site zinc ligands are all histidines (His-218, His-222, and His-228). The presence of a second zinc ion in a structural role is a unique feature of the matrix metalloproteinases. The binding properties of the active site cleft are more dependent on the main chain conformation of the enzyme (and substrate) compared with thermolysin. A mechanism of action for peptide cleavage similar to that of thermolysin is proposed for fibroblast collagenase. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, CA and PLH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http:// | + | 1HFC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PLH:'>PLH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Interstitial collagenase]] | [[Category: Interstitial collagenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Smith, D | + | [[Category: Smith, D L.]] |
| - | [[Category: Spurlino, J | + | [[Category: Spurlino, J C.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: PLH]] | [[Category: PLH]] | ||
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[[Category: metalloprotease]] | [[Category: metalloprotease]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:46 2008'' |
Revision as of 11:00, 21 February 2008
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1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE
Contents |
Overview
The X-ray crystal structure of a 19 kDa active fragment of human fibroblast collagenase has been determined by the multiple isomorphous replacement method and refined at 1.56 A resolution to an R-factor of 17.4%. The current structure includes a bound hydroxamate inhibitor, 88 waters and three metal atoms (two zincs and a calcium). The overall topology of the enzyme, comprised of a five stranded beta-sheet and three alpha-helices, is similar to the thermolysin-like metalloproteinases. There are some important differences between the collagenase and thermolysin families of enzymes. The active site zinc ligands are all histidines (His-218, His-222, and His-228). The presence of a second zinc ion in a structural role is a unique feature of the matrix metalloproteinases. The binding properties of the active site cleft are more dependent on the main chain conformation of the enzyme (and substrate) compared with thermolysin. A mechanism of action for peptide cleavage similar to that of thermolysin is proposed for fibroblast collagenase.
Disease
Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]
About this Structure
1HFC is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.
Reference
1.56 A structure of mature truncated human fibroblast collagenase., Spurlino JC, Smallwood AM, Carlton DD, Banks TM, Vavra KJ, Johnson JS, Cook ER, Falvo J, Wahl RC, Pulvino TA, et al., Proteins. 1994 Jun;19(2):98-109. PMID:8090713
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