1z5h
From Proteopedia
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| - | [[Image:1z5h.gif|left|200px]] | + | [[Image:1z5h.gif|left|200px]] |
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| - | '''Crystal structures of the Tricorn interacting Factor F3 from Thermoplasma acidophilum''' | + | {{Structure |
| + | |PDB= 1z5h |SIZE=350|CAPTION= <scene name='initialview01'>1z5h</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structures of the Tricorn interacting Factor F3 from Thermoplasma acidophilum''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z5H is a [ | + | 1Z5H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5H OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations., Kyrieleis OJ, Goettig P, Kiefersauer R, Huber R, Brandstetter H, J Mol Biol. 2005 Jun 17;349(4):787-800. Epub 2005 Apr 26. PMID:[http:// | + | Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations., Kyrieleis OJ, Goettig P, Kiefersauer R, Huber R, Brandstetter H, J Mol Biol. 2005 Jun 17;349(4):787-800. Epub 2005 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15893768 15893768] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| - | [[Category: | + | [[Category: gluzicin]] |
[[Category: superhelix]] | [[Category: superhelix]] | ||
[[Category: tricorn protease]] | [[Category: tricorn protease]] | ||
[[Category: zinc aminopeptidase]] | [[Category: zinc aminopeptidase]] | ||
| - | ''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 15:31:24 2008'' |
Revision as of 13:31, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structures of the Tricorn interacting Factor F3 from Thermoplasma acidophilum
Overview
The tricorn interacting factor F3 is an 89 kDa zinc aminopeptidase from the archaeon Thermoplasma acidophilum. Together with the tricorn interacting factors F1 and F2, F3 degrades the tricorn protease products and thus completes the proteasomal degradation pathway by generating free amino acids. Here, we present the crystal structures of F3 in three different conformations at 2.3 A resolution. The zinc aminopeptidase is composed of four domains: an N-terminal saddle-like beta-structure domain; a thermolysin-like catalytic domain; a small barrel-like beta-structure domain; and an alpha-helical C-terminal domain, the latter forming a deep cavity at the active site. Three crystal forms provide snapshots of the molecular dynamics of F3 where the C-terminal domain can adapt to form an open, an intermediate and a nearly closed cavity, respectively. With the conserved Zn(2+)-binding motifs HEXXH and NEXFA as well as the N-terminal substrate-anchoring glutamate residues, F3 together with the leukotriene A4 hydrolase, represents a novel gluzincin subfamily of aminoproteases. We discuss the functional implications of these structures with respect to the underlying catalytic mechanism, substrate recognition and processing, and possible component interactions.
About this Structure
1Z5H is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations., Kyrieleis OJ, Goettig P, Kiefersauer R, Huber R, Brandstetter H, J Mol Biol. 2005 Jun 17;349(4):787-800. Epub 2005 Apr 26. PMID:15893768
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