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[[Image:1fwd.gif|left|200px]]


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==KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 9.4==
The line below this paragraph, containing "STRUCTURE_1fwd", creates the "Structure Box" on the page.
<StructureSection load='1fwd' size='340' side='right'caption='[[1fwd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fwd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FWD FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
{{STRUCTURE_1fwd|  PDB=1fwd |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fwd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fwd OCA], [https://pdbe.org/1fwd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fwd RCSB], [https://www.ebi.ac.uk/pdbsum/1fwd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fwd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/URE3_KLEAE URE3_KLEAE]
== 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/fw/1fwd_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=1fwd ConSurf].
<div style="clear:both"></div>


'''KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 9.4'''
==See Also==
 
*[[Urease 3D structures|Urease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Cys319 is located on a mobile flap covering the active site of Klebsiella aerogenes urease but does not play an essential role in catalysis. Four urease variants altered at position C319 range from having high activity (C319A) to no measurable activity (C319Y), indicating Cys is not required at this position, but its presence is highly influential [Martin, P. R., &amp; Hausinger, R. P. (1992) J. Biol. Chem. 267, 20024-20027]. Here, we present 2.0 A resolution crystal structures of C319A, C319S, C319D, and C319Y proteins and the C319A variant inhibited by acetohydroxamic acid. These structures show changes in the hydration of the active site nickel ions and in the position and flexibility of the active site flap. The C319Y protein exhibits an alternate conformation of the flap, explaining its lack of activity. The changes in hydration and conformation suggest that there are suboptimal protein-solvent and protein-protein interactions in the empty urease active site which contribute to urease catalysis. Specifically, we hypothesize that the suboptimal interactions may provide a significant source of substrate binding energy, and such hidden energy may be a common phenomenon for enzymes that contain mobile active site loops and undergo an induced fit. The acetohydroxamic acid-bound structure reveals a chelate interaction similar to those seen in other metalloenzymes and in a small molecule nickel complex. The inhibitor binding mode supports the proposed mode of urea binding. We complement these structural studies with extended functional studies of C319A urease to show that it has enhanced stability and resistance to inhibition by buffers containing nickel ions. The near wild-type activity and enhanced stability of the C319A variant make it useful for further studies of urease structure-function relationships.
 
==About this Structure==
1FWD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FWD OCA].
 
==Reference==
Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease., Pearson MA, Michel LO, Hausinger RP, Karplus PA, Biochemistry. 1997 Jul 1;36(26):8164-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9201965 9201965]
[[Category: Klebsiella aerogenes]]
[[Category: Klebsiella aerogenes]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Urease]]
[[Category: Karplus PA]]
[[Category: Karplus, P A.]]
[[Category: Pearson MA]]
[[Category: Pearson, M A.]]
[[Category: Mutant]]
[[Category: Nickel metalloenzyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:50:33 2008''

Latest revision as of 14:17, 27 March 2024

KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 9.4KLEBSIELLA AEROGENES UREASE, C319A VARIANT AT PH 9.4

Structural highlights

1fwd is a 3 chain structure with sequence from Klebsiella aerogenes. 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

URE3_KLEAE

Evolutionary Conservation

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

See Also

1fwd, resolution 2.00Å

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