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| {{STRUCTURE_1xfo| PDB=1xfo | SCENE= }} | | {{STRUCTURE_1xfo| PDB=1xfo | SCENE= }} |
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| '''Crystal Structure of an archaeal aminopeptidase'''
| | ===Crystal Structure of an archaeal aminopeptidase=== |
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| ==Overview==
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| Protein turnover is an essential process in living cells. The degradation of cytosolic polypeptides is mainly carried out by the proteasome, resulting in 7-9-amino acid long peptides. Further degradation is usually carried out by energy-independent proteases like the tricorn protease from Thermoplasma acidophilum. Recently, a novel tetrahedral-shaped dodecameric 480-kDa aminopeptidase complex (TET) has been described in Haloarcula marismortui that differs from the known ring- or barrel-shaped self-compartmentalizing proteases. This complex is capable of degrading most peptides down to amino acids. We present here the crystal structure of the tetrahedral aminopeptidase homolog FrvX from Pyrococcus horikoshii. The monomer has a typical clan MH fold, as found for example in Aeromonas proteolytica aminopeptidase, containing a dinuclear zinc active center. The quaternary structure is built by dimers with a length of 100 A that form the edges of the tetrahedron. All 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by pores with a maximal diameter of 10 A, allowing only small peptides and unfolded proteins access to the active site.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15375159}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15375159 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15375159}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Self-compartmentalizing]] | | [[Category: Self-compartmentalizing]] |
| [[Category: X-ray diffraction]] | | [[Category: X-ray diffraction]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:58:12 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:29:37 2008'' |
