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3pga

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[[Image:3pga.jpg|left|200px]]
 
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{{Structure
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==STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE==
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|PDB= 3pga |SIZE=350|CAPTION= <scene name='initialview01'>3pga</scene>, resolution 2.0&Aring;
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<StructureSection load='3pga' size='340' side='right'caption='[[3pga]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=UNK:UNKNOWN'>UNK</scene>
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<table><tr><td colspan='2'>[[3pga]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._7A Pseudomonas sp. 7A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PGA FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </span>
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</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&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pga OCA], [https://pdbe.org/3pga PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pga RCSB], [https://www.ebi.ac.uk/pdbsum/3pga PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pga ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pga OCA], [http://www.ebi.ac.uk/pdbsum/3pga PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3pga RCSB]</span>
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[https://www.uniprot.org/uniprot/ASPQ_PSES7 ASPQ_PSES7]
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pg/3pga_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3pga ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE'''
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==See Also==
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*[[Glutaminase 3D structures|Glutaminase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The amino acid sequence and a 2-A-resolution crystallographic structure of Pseudomonas 7A glutaminase-asparaginase (PGA) have been determined. PGA, which belongs to the family of tetrameric bacterial amidohydrolases, deamidates glutamine and asparagine. The amino acid sequence of PGA has a high degree of similarity to the sequences of other members of the family. PGA has the same fold as other bacterial amidohydrolases, with the exception of the position of a 20-residue loop that forms part of the active site. In the PGA structure presented here, the active site loop is observed clearly in only one monomer, in an open position, with a conformation different from that observed for other amidohydrolases. In the other three monomers the loop is disordered and cannot be traced. This phenomenon is probably a direct consequence of a very low occupancy of product(s) of the enzymatic reaction bound in the active sites of PGA in these crystals. The active sites are composed of a rigid part and the flexible loop. The rigid part consists of the residues directly involved in the catalytic reaction as well as residues that assist in orienting the substrate. Two residues that are important for activity residue on the flexible loop. We suggest that the flexible loops actively participate in the transport of substrate and product molecules through the amidohydrolase active sites and participate in orienting the substrate molecules properly in relation to the catalytic residues.
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. 7A]]
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==About this Structure==
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[[Category: Ammon HL]]
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3PGA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._7a Pseudomonas sp. 7a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGA OCA].
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[[Category: Copeland TD]]
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[[Category: Lubkowski J]]
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==Reference==
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[[Category: Swain AL]]
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Structural characterization of Pseudomonas 7A glutaminase-asparaginase., Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL, Biochemistry. 1994 Aug 30;33(34):10257-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8068664 8068664]
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[[Category: Wlodawer A]]
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[[Category: Asparaginase]]
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[[Category: Pseudomonas sp. 7a]]
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[[Category: Single protein]]
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[[Category: Ammon, H L.]]
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[[Category: Copeland, T D.]]
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[[Category: Lubkowski, J.]]
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[[Category: Swain, A L.]]
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[[Category: Wlodawer, A.]]
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[[Category: bacterial amidohydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:35:23 2008''
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Current revision

STRUCTURAL CHARACTERIZATION OF PSEUDOMONAS 7A GLUTAMINASE-ASPARAGINASE

PDB ID 3pga

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