1xgs: Difference between revisions
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[[Image:1xgs. | [[Image:1xgs.jpg|left|200px]]<br /><applet load="1xgs" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1xgs" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1xgs, resolution 1.75Å" /> | caption="1xgs, resolution 1.75Å" /> | ||
'''METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS'''<br /> | '''METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1XGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. | 1XGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with CO as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=ACA:Side Chains Of Five Amino Acid Residues ASP 82, ASP 93, ...'>ACA</scene> and <scene name='pdbsite=ACB:Side Chains Of Five Amino Acid Residues ASP 82, ASP 93, ...'>ACB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XGS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hyperthermophile]] | [[Category: hyperthermophile]] | ||
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Revision as of 19:29, 18 December 2007
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METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS
OverviewOverview
The structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus (PfMAP) with an optimal growth temperature of 100, degreesC was determined by the multiple isomorphous replacement method and, refined in three different crystal forms, one monoclinic and two, hexagonal, at resolutions of 2.8, 2.9, and 3.5 A. The resolution of the, monoclinic crystal form was extended to 1.75 A by water-mediated, transformation to a low-humidity form, and the obtained diffraction data, used for high-resolution structure refinement. This is the first, description of a eukaryotic type methionine aminopeptidase structure. The, PfMAP molecule is composed of two domains, a catalytic domain and an, insertion domain, connected via two antiparallel beta-strands. The, catalytic domain, which possesses an internal 2-fold symmetry and contains, two cobalt ions in the active site, resembles the structure of a, prokaryotic type MAP from Escherichia coli (EcMAP), while the structure of, the insertion domain containing three helices has a novel fold and, accounts for a major difference between the eukaryotic and prokaryotic, types of methionine aminopeptidase. Analysis of the PfMAP structure in, comparison with EcMAP and other mesophile proteins reveals several factors, which may contribute to the hyperthermostability of PfMAP: (1) a, significantly high number of hydrogen bonds and ion-pairs between, side-chains of oppositely charged residues involved in the stabilization, of helices; (2) an increased number of hydrogen bonds between the, positively charged side-chain and neutral oxygen; (3) a larger number of, buried water molecules involved in crosslinking the backbone atoms of, sequentially separate segments; (4) stabilization of two antiparallel, beta-strands connecting the two domains of the molecule by proline, residues; (5) shortening of N and C-terminal tails and stabilization of, the loop c3E by deletion of three residues.
About this StructureAbout this Structure
1XGS is a Single protein structure of sequence from Pyrococcus furiosus with CO as ligand. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus., Tahirov TH, Oki H, Tsukihara T, Ogasahara K, Yutani K, Ogata K, Izu Y, Tsunasawa S, Kato I, J Mol Biol. 1998 Nov 20;284(1):101-24. PMID:9811545
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