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New page: left|200px<br /><applet load="1rzy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzy, resolution 1.80Å" /> '''Crystal structure of...
 
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[[Image:1rzy.jpg|left|200px]]<br /><applet load="1rzy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rzy, resolution 1.80&Aring;" />
'''Crystal structure of rabbit Hint complexed with N-ethylsulfamoyladenosine'''<br />


==Overview==
==Crystal structure of rabbit Hint complexed with N-ethylsulfamoyladenosine==
Hint, histidine triad nucleotide-binding protein, is a universally, conserved enzyme that hydrolyzes AMP linked to lysine and, in yeast, functions as a positive regulator of the RNA polymerase II C-terminal, domain kinase, Kin28. To explore the biochemical and structural bases for, the adenosine phosphoramidate hydrolase activity of rabbit Hint, we, synthesized novel substrates linking a p-nitroaniline group to adenylate, (AMP-pNA) and inhibitors that consist of an adenosine group and, 5'-sulfamoyl (AdoOSO(2)NH(2)) or N-ethylsulfamoyl (AdoOSO(2)NHCH(2)CH(3)), group. AMP-pNA is a suitable substrate for Hint that allowed, characterization of the inhibitors; titration of each inhibitor into, AMP-pNA assays revealed their K(i) values. The N-ethylsulfamoyl derivative, has a 13-fold binding advantage over the sulfamoyl adenosine. The 1.8-A, cocrystal structure of rabbit Hint with N-ethylsulfamoyl adenosine, revealed a binding site for the ethyl group against Trp-123, a residue, that reaches across the Hint dimer interface to interact with the alkyl, portion of the inhibitor and, presumably, the alkyl portion of a lysyl, substrate. Ser-107 is positioned to donate a hydrogen bond to the leaving, group nitrogen. Consistent with a role in acid-base catalysis, the Hint, S107A mutant protein displayed depressed catalytic activity.
<StructureSection load='1rzy' size='340' side='right'caption='[[1rzy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1rzy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RZY 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AS:5-O-(N-ETHYL-SULFAMOYL)ADENOSINE'>5AS</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=1rzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rzy OCA], [https://pdbe.org/1rzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rzy RCSB], [https://www.ebi.ac.uk/pdbsum/1rzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rzy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HINT1_RABIT HINT1_RABIT] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2.
== 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/rz/1rzy_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=1rzy ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1RZY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with 5AS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RZY OCA].
*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Biochemical, crystallographic, and mutagenic characterization of hint, the AMP-lysine hydrolase, with novel substrates and inhibitors., Krakowiak A, Pace HC, Blackburn GM, Adams M, Mekhalfia A, Kaczmarek R, Baraniak J, Stec WJ, Brenner C, J Biol Chem. 2004 Apr 30;279(18):18711-6. Epub 2004 Feb 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14982931 14982931]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Single protein]]
[[Category: Adams M]]
[[Category: Adams, M.]]
[[Category: Baraniak J]]
[[Category: Baraniak, J.]]
[[Category: Blackburn GM]]
[[Category: Blackburn, G.M.]]
[[Category: Brenner C]]
[[Category: Brenner, C.]]
[[Category: Kaczmarek R]]
[[Category: Kaczmarek, R.]]
[[Category: Krakowiak AK]]
[[Category: Krakowiak, A.K.]]
[[Category: Mekhalfia A]]
[[Category: Mekhalfia, A.]]
[[Category: Pace HC]]
[[Category: Pace, H.C.]]
[[Category: Stec WJ]]
[[Category: Stec, W.J.]]
[[Category: 5AS]]
[[Category: hit protein; protein-inhibitor complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:59:40 2007''
Retrieved from "https://proteopedia.org/1rzy"