1mt3
From Proteopedia
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| - | [[Image:1mt3.jpg|left|200px]] | + | [[Image:1mt3.jpg|left|200px]] |
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| - | '''Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1''' | + | {{Structure |
| + | |PDB= 1mt3 |SIZE=350|CAPTION= <scene name='initialview01'>1mt3</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] | ||
| + | |GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MT3 is a [ | + | 1MT3 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=1MT3 OCA]. |
==Reference== | ==Reference== | ||
| - | Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism., Goettig P, Groll M, Kim JS, Huber R, Brandstetter H, EMBO J. 2002 Oct 15;21(20):5343-52. PMID:[http:// | + | Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism., Goettig P, Groll M, Kim JS, Huber R, Brandstetter H, EMBO J. 2002 Oct 15;21(20):5343-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12374735 12374735] |
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: prolylpeptidase]] | [[Category: prolylpeptidase]] | ||
| - | ''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 12:47:49 2008'' |
Revision as of 10:47, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Gene: | TA0830 (Thermoplasma acidophilum) | ||||||
| Activity: | Prolyl aminopeptidase, with EC number 3.4.11.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1
Overview
F1 is a 33.5 kDa serine peptidase of the alpha/beta-hydrolase family from the archaeon Thermoplasma acidophilum. Subsequent to proteasomal protein degradation, tricorn generates small peptides, which are cleaved by F1 to yield single amino acids. We have solved the crystal structure of F1 with multiwavelength anomalous dispersion (MAD) phasing at 1.8 A resolution. In addition to the conserved catalytic domain, the structure reveals a chiefly alpha-helical domain capping the catalytic triad. Thus, the active site is accessible only through a narrow opening from the protein surface. Two structures with molecules bound to the active serine, including the inhibitor phenylalanyl chloromethylketone, elucidate the N-terminal recognition of substrates and the catalytic activation switch mechanism of F1. The cap domain mainly confers the specificity for hydrophobic side chains by a novel cavity system, which, analogously to the tricorn protease, guides substrates to the buried active site and products away from it. Finally, the structure of F1 suggests a possible functional complex with tricorn that allows efficient processive degradation to free amino acids for cellular recycling.
About this Structure
1MT3 is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
Reference
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism., Goettig P, Groll M, Kim JS, Huber R, Brandstetter H, EMBO J. 2002 Oct 15;21(20):5343-52. PMID:12374735
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