1iut: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1iut" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iut, resolution 2.0Å" /> '''P-HYDROXYBENZOATE HYD...
 
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1iut.jpg|left|200px]]<br /><applet load="1iut" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1iut, resolution 2.0&Aring;" />
'''P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 7.4'''<br />


==Overview==
==P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 7.4==
Deprotonation of p-hydroxybenzoate to the phenolate and reprotonation of, the hydroxylated dienone intermediate to form the product are essential, steps in the reaction catalyzed by p-hydroxybenzoate hydroxylase (PHBH)., The mechanism by which protons are transferred in these reactions is not, obvious, because the substrate bound in the active site is isolated from, solvent. Structure analyses of wild-type and mutant PHBH, with bound, p-hydroxybenzoate or p-aminobenzoate, reveal a chain of proton donors and, acceptors (the hydroxyl groups of Tyr201 and Tyr385, and two water, molecules) that can connect the substrate 4-OH to His72, a surface, residue. This chain could provide a pathway for proton transfer to and, from the substrate. Using various combinations of pH and substrates, we, show that in crystalline PHBH ionizable groups in the chain may rotate and, change hydrogen-bond orientation. Molecular dynamics simulations have been, used to predict the preferred orientation of hydrogen bonds in the chain, as a function of the ionization states of substrate and His72. The, calculations suggest that changes in the ionization state of the substrate, could be associated with changes in orientation of the hydrogen bonds in, the chain. Transfer of water between the chain of proton donors and the, solvent also appears to be an essential part of the mechanism that, provides reversible transfer of protons during the hydroxylation reaction.
<StructureSection load='1iut' size='340' side='right'caption='[[1iut]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1iut]] 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=1IUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IUT 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=PAB:4-AMINOBENZOIC+ACID'>PAB</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=1iut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iut OCA], [https://pdbe.org/1iut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iut RCSB], [https://www.ebi.ac.uk/pdbsum/1iut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iut 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/iu/1iut_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=1iut ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IUT 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 FAD and PAB 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=1IUT OCA].
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis., Gatti DL, Entsch B, Ballou DP, Ludwig ML, Biochemistry. 1996 Jan 16;35(2):567-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8555229 8555229]
[[Category: Large Structures]]
[[Category: 4-hydroxybenzoate 3-monooxygenase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Ballou DP]]
[[Category: Ballou, D.P.]]
[[Category: Entsch B]]
[[Category: Entsch, B.]]
[[Category: Gatti DL]]
[[Category: Gatti, D.L.]]
[[Category: Ludwig ML]]
[[Category: Ludwig, M.L.]]
[[Category: FAD]]
[[Category: PAB]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:40:56 2007''

Latest revision as of 10:37, 7 February 2024

P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 7.4P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 7.4

Structural highlights

1iut 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

1iut, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1iut&oldid=4045113"