3pga

<table><tr><td colspan='2'>[[3pga]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_7a Pseudomonas 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PGA FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/3pga PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pga RCSB], [http://www.ebi.ac.uk/pdbsum/3pga PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pga ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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:8068664<ref>PMID:8068664</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Glutaminase-Asparaginase (Pseudomonas 7A)|Glutaminase-Asparaginase (Pseudomonas 7A)]]

== References ==

<references/>

[[Category: Asparaginase]]

[[Category: Pseudomonas 7a]]

[[Category: Ammon, H L]]

[[Category: Copeland, T D]]

[[Category: Lubkowski, J]]

[[Category: Swain, A L]]

[[Category: Wlodawer, A]]

[[Category: Bacterial amidohydrolase]]