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New page: left|200px<br /><applet load="2ip2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ip2, resolution 1.80Å" /> '''Structure of the Pyo...
 
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[[Image:2ip2.jpg|left|200px]]<br /><applet load="2ip2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ip2, resolution 1.80&Aring;" />
'''Structure of the Pyocyanin Biosynthetic Protein PhzM'''<br />


==Overview==
==Structure of the Pyocyanin Biosynthetic Protein PhzM==
Pyocyanin is a biologically active phenazine produced by the human, pathogen Pseudomonas aeruginosa. It is thought to endow P. aeruginosa with, a competitive growth advantage in colonized tissue and is also thought to, be a virulence factor in diseases such as cystic fibrosis and AIDS where, patients are commonly infected by pathogenic Pseudomonads due to their, immunocompromised state. Pyocyanin is also a chemically interesting, compound due to its unusual oxidation-reduction activity., Phenazine-1-carboxylic acid, the precursor to the bioactive phenazines, is, synthesized from chorismic acid by enzymes encoded in a seven-gene cistron, in P. aeruginosa and in other Pseudomonads. Phenzine-1-carboxylic acid is, believed to be converted to pyocyanin by the sequential actions of the, putative S-adenosylmethionine-dependent N-methyltransferase PhzM and the, putative flavin-dependent hydroxylase PhzS. Here we report the 1.8 A, crystal structure of PhzM determined by single anomalous dispersion., Unlike many methyltransferases, PhzM is a dimer in solution. The 36 kDa, PhzM polypeptide folds into three domains. The C-terminal domain exhibits, the alpha/beta-hydrolase fold typical of small molecule, methyltransferases. Two smaller N-terminal domains form much of the dimer, interface. Structural alignments with known methyltransferases show that, PhzM is most similar to the plant O-methyltransferases that are, characterized by an unusual intertwined dimer interface. The structure of, PhzM contains no ligands, and the active site is open and solvent-exposed, when compared to structures of similar enzymes. In vitro experiments using, purified PhzM alone demonstrate that it has little or no ability to, methylate phenzine-1-carboxylic acid. However, when the putative, hydroxylase PhzS is included, pyocyanin is readily produced. This, observation suggests that a mechanism has evolved in P. aeruginosa that, ensures efficient production of pyocyanin via the prevention of the, formation and release of an unstable and potentially deleterious, intermediate.
<StructureSection load='2ip2' size='340' side='right'caption='[[2ip2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2ip2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IP2 FirstGlance]. <br>
2IP2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IP2 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=2ip2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ip2 OCA], [https://pdbe.org/2ip2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ip2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ip2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ip2 ProSAT]</span></td></tr>
==Reference==
</table>
Structural and functional analysis of the pyocyanin biosynthetic protein PhzM from Pseudomonas aeruginosa., Parsons JF, Greenhagen BT, Shi K, Calabrese K, Robinson H, Ladner JE, Biochemistry. 2007 Feb 20;46(7):1821-8. Epub 2007 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17253782 17253782]
== Function ==
[[Category: Pseudomonas aeruginosa]]
[https://www.uniprot.org/uniprot/PHZM_PSEAE PHZM_PSEAE] Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Converts phenazine-1-carboxylate (PCA) to 5-methylphenazine-1-carboxylate (5-methyl-PCA).<ref>PMID:17253782</ref>
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Ladner, J.E.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Parsons, J.F.]]
Check<jmol>
[[Category: Robinson, H.]]
  <jmolCheckbox>
[[Category: Shi, K.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/2ip2_consurf.spt"</scriptWhenChecked>
[[Category: methyltransferase]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: phenazine]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: phenazine-1-carboxylic acid]]
  </jmolCheckbox>
[[Category: phzm]]
</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=2ip2 ConSurf].
[[Category: pyocyanin]]
<div style="clear:both"></div>
 
== References ==
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:48:59 2008''
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Ladner JE]]
[[Category: Parsons JF]]
[[Category: Robinson H]]
[[Category: Shi K]]
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