1cg2: Difference between revisions

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New page: left|200px<br /> <applet load="1cg2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cg2, resolution 2.5Å" /> '''CARBOXYPEPTIDASE G2'...
 
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[[Image:1cg2.gif|left|200px]]<br />
<applet load="1cg2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1cg2, resolution 2.5&Aring;" />
'''CARBOXYPEPTIDASE G2'''<br />


==Overview==
==CARBOXYPEPTIDASE G2==
BACKGROUND: Carboxypeptidase G enzymes hydrolyze the C-terminal glutamate, moiety from folic acid and its analogues, such as methotrexate. The enzyme, studied here, carboxypeptidase G2 (CPG2), is a dimeric zinc-dependent, exopeptidase produced by Pseudomonas sp. strain RS-16. CPG2 has, applications in cancer therapy: following its administration as an, immunoconjugate, in which CPG2 is linked to an antibody to a, tumour-specific antigen, it can enzymatically convert subsequently, administered inactive prodrugs to cytotoxic drugs selectively at the, tumour site. CPG2 has no significant amino acid sequence homology with, proteins of known structure. Hence, structure determination of CPG2 was, undertaken to identify active-site residues, which may in turn provide, ideas for protein and/or ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9083113 (full description)]]
<StructureSection load='1cg2' size='340' side='right'caption='[[1cg2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1cg2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._RS-16 Pseudomonas sp. RS-16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CG2 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1cg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cg2 OCA], [https://pdbe.org/1cg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cg2 RCSB], [https://www.ebi.ac.uk/pdbsum/1cg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cg2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBPG_PSES6 CBPG_PSES6] Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
== 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/cg/1cg2_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=1cg2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CG2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.11 3.4.17.11]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CG2 OCA]].
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy., Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P, Structure. 1997 Mar 15;5(3):337-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9083113 9083113]
[[Category: Large Structures]]
[[Category: Pseudomonas sp.]]
[[Category: Pseudomonas sp. RS-16]]
[[Category: Single protein]]
[[Category: Blow DM]]
[[Category: Blow, D.M.]]
[[Category: Brick P]]
[[Category: Brick, P.]]
[[Category: Melton RG]]
[[Category: Melton, R.G.]]
[[Category: Pauptit RA]]
[[Category: Pauptit, R.A.]]
[[Category: Rowsell S]]
[[Category: Rowsell, S.]]
[[Category: Tucker AD]]
[[Category: Tucker, A.D.]]
[[Category: ZN]]
[[Category: hydrolase]]
[[Category: metallocarboxypeptidase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:50:01 2007''

Latest revision as of 10:24, 14 February 2024

CARBOXYPEPTIDASE G2CARBOXYPEPTIDASE G2

Structural highlights

1cg2 is a 4 chain structure with sequence from Pseudomonas sp. RS-16. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBPG_PSES6 Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.

Evolutionary Conservation

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

See Also

1cg2, resolution 2.50Å

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