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[[Image:1xgs.jpg|left|200px]]<br /><applet load="1xgs" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1xgs, resolution 1.75&Aring;" />
'''METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS'''<br />


==Overview==
==METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS==
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.
<StructureSection load='1xgs' size='340' side='right'caption='[[1xgs]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xgs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgs OCA], [https://pdbe.org/1xgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgs RCSB], [https://www.ebi.ac.uk/pdbsum/1xgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAP2_PYRFU MAP2_PYRFU] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).[HAMAP-Rule:MF_01975]<ref>PMID:9399590</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xg/1xgs_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xgs ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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 <scene name='pdbligand=CO:'>CO</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGS OCA].
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9811545 9811545]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Tahirov TH]]
[[Category: Tahirov, T.H.]]
[[Category: Tsukihara T]]
[[Category: Tsukihara, T.]]
[[Category: CO]]
[[Category: aminopeptidase]]
[[Category: hyperthermophile]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:22:04 2008''

Latest revision as of 11:50, 14 February 2024

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUSMETHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

Structural highlights

1xgs is a 2 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.75Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAP2_PYRFU Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).[HAMAP-Rule:MF_01975][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Tsunasawa S, Izu Y, Miyagi M, Kato I. Methionine aminopeptidase from the hyperthermophilic Archaeon Pyrococcus furiosus: molecular cloning and overexpression in Escherichia coli of the gene, and characteristics of the enzyme. J Biochem. 1997 Oct;122(4):843-50. PMID:9399590 doi:10.1093/oxfordjournals.jbchem.a021831

1xgs, resolution 1.75Å

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