1xfo
From Proteopedia
(New page: 200px<br /><applet load="1xfo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xfo, resolution 1.96Å" /> '''Crystal Structure of...) |
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| - | [[Image:1xfo.gif|left|200px]]<br /><applet load="1xfo" size=" | + | [[Image:1xfo.gif|left|200px]]<br /><applet load="1xfo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xfo, resolution 1.96Å" /> | caption="1xfo, resolution 1.96Å" /> | ||
'''Crystal Structure of an archaeal aminopeptidase'''<br /> | '''Crystal Structure of an archaeal aminopeptidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein turnover is an essential process in living cells. The degradation | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1XFO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1XFO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:16 2008'' |
Revision as of 13:54, 21 February 2008
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Crystal Structure of an archaeal aminopeptidase
Overview
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.
About this Structure
1XFO is a Single protein structure of sequence from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase., Russo S, Baumann U, J Biol Chem. 2004 Dec 3;279(49):51275-81. Epub 2004 Sep 16. PMID:15375159
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