1k0l: Difference between revisions

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New page: left|200px<br /><applet load="1k0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k0l, resolution 2.0Å" /> '''Pseudomonas aeruginos...
 
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[[Image:1k0l.jpg|left|200px]]<br /><applet load="1k0l" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1k0l, resolution 2.0&Aring;" />
'''Pseudomonas aeruginosa phbh R220Q free of p-OHB'''<br />


==Overview==
==Pseudomonas aeruginosa phbh R220Q free of p-OHB==
para-Hydroxybenzoate hydroxylase catalyzes a two-step reaction that, demands precise control of solvent access to the catalytic site. The first, step of the reaction, reduction of flavin by NADPH, requires access to, solvent. The second step, oxygenation of reduced flavin to a flavin, C4a-hydroperoxide that transfers the hydroxyl group to the substrate, requires that solvent be excluded to prevent breakdown of the, hydroperoxide to oxidized flavin and hydrogen peroxide. These conflicting, requirements are met by the coordination of multiple movements involving, the protein, the two cofactors, and the substrate. Here, using the R220Q, mutant form of para-hydroxybenzoate hydroxylase, we show that in the, absence of substrate, the large beta alpha beta domain (residues 1-180), and the smaller sheet domain (residues 180-270) separate slightly, and the, flavin swings out to a more exposed position to open an aqueous channel, from the solvent to the protein interior. Substrate entry occurs by first, binding at a surface site and then sliding into the protein interior. In, our study of this mutant, the structure of the complex with pyridine, nucleotide was obtained. This cofactor binds in an extended conformation, at the enzyme surface in a groove that crosses the binding site of FAD. We, postulate that for stereospecific reduction, the flavin swings to an out, position and NADPH assumes a folded conformation that brings its, nicotinamide moiety into close contact with the isoalloxazine moiety of, the flavin. This work clearly shows how complex dynamics can play a, central role in catalysis by enzymes.
<StructureSection load='1k0l' size='340' side='right'caption='[[1k0l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1k0l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0L 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1k0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0l OCA], [https://pdbe.org/1k0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0l RCSB], [https://www.ebi.ac.uk/pdbsum/1k0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0l ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHHY_PSEAE PHHY_PSEAE]
== 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/k0/1k0l_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=1k0l ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1K0L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with SO4, SO3 and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxybenzoate_3-monooxygenase 4-hydroxybenzoate 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.2 1.14.13.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K0L OCA].
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase., Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL, Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):608-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11805318 11805318]
[[Category: Large Structures]]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Ballou D]]
[[Category: Ballou, D.]]
[[Category: Entsch B]]
[[Category: Entsch, B.]]
[[Category: Gatti DL]]
[[Category: Gatti, D.L.]]
[[Category: Ortiz-Maldonado M]]
[[Category: Ortiz-Maldonado, M.]]
[[Category: Wang J]]
[[Category: Wang, J.]]
[[Category: FAD]]
[[Category: SO3]]
[[Category: SO4]]
[[Category: fad]]
[[Category: mechanism]]
[[Category: phbh]]
[[Category: structure]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:45:28 2007''

Latest revision as of 10:43, 7 February 2024

Pseudomonas aeruginosa phbh R220Q free of p-OHBPseudomonas aeruginosa phbh R220Q free of p-OHB

Structural highlights

1k0l is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHHY_PSEAE

Evolutionary Conservation

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

See Also

1k0l, resolution 2.00Å

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