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[[Image:1ka4.jpg|left|200px]]<br /><applet load="1ka4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ka4, resolution 3.00&Aring;" />
'''Structure of Pyrococcus furiosus carboxypeptidase Nat-Pb'''<br />


==Overview==
==Structure of Pyrococcus furiosus carboxypeptidase Nat-Pb==
The structure of Pyrococcus furiosus carboxypeptidase (PfuCP) has been determined to 2.2 A resolution using multiwavelength anomalous diffraction (MAD) methods. PfuCP represents the first structure of the new M32 family of carboxypeptidases. The overall structure is comprised of a homodimer. Each subunit is mostly helical with its most pronounced feature being a deep substrate binding groove. The active site lies at the bottom of this groove and contains an HEXXH motif that coordinates the metal ion required for catalysis. Surprisingly, the structure is similar to the recently reported rat neurolysin. Comparison of these structures as well as sequence analyses with other homologous proteins reveal several conserved residues. The roles for these conserved residues in the catalytic mechanism are inferred based on modeling and their location.
<StructureSection load='1ka4' size='340' side='right'caption='[[1ka4]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ka4]] is a 1 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=1KA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KA4 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PB:LEAD+(II)+ION'>PB</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=1ka4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ka4 OCA], [https://pdbe.org/1ka4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ka4 RCSB], [https://www.ebi.ac.uk/pdbsum/1ka4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ka4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBP1_PYRFU CBP1_PYRFU] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.<ref>PMID:10595552</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/ka/1ka4_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=1ka4 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KA4 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=PB:'>PB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KA4 OCA].
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
== References ==
==Reference==
<references/>
Crystal structure of a novel carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus., Arndt JW, Hao B, Ramakrishnan V, Cheng T, Chan SI, Chan MK, Structure. 2002 Feb;10(2):215-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11839307 11839307]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Arndt JW]]
[[Category: Arndt, J W.]]
[[Category: Chan MK]]
[[Category: Chan, M K.]]
[[Category: Chan SI]]
[[Category: Chan, S I.]]
[[Category: Cheng T]]
[[Category: Cheng, T.]]
[[Category: Hao B]]
[[Category: Hao, B.]]
[[Category: Ramakrishnan V]]
[[Category: Ramakrishnan, V.]]
[[Category: PB]]
[[Category: hexxh motif]]
[[Category: m32 family]]
[[Category: metallopeptidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:45 2008''

Latest revision as of 10:45, 7 February 2024

Structure of Pyrococcus furiosus carboxypeptidase Nat-PbStructure of Pyrococcus furiosus carboxypeptidase Nat-Pb

Structural highlights

1ka4 is a 1 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 3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBP1_PYRFU Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro, Gly, Asp and Glu.[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. Cheng TC, Ramakrishnan V, Chan SI. Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus. Protein Sci. 1999 Nov;8(11):2474-86. PMID:10595552 doi:http://dx.doi.org/10.1110/ps.8.11.2474

1ka4, resolution 3.00Å

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