1av5

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[[Image:1av5.gif|left|200px]]
 
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{{Structure
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==PKCI-SUBSTRATE ANALOG==
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|PDB= 1av5 |SIZE=350|CAPTION= <scene name='initialview01'>1av5</scene>, resolution 2.0&Aring;
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<StructureSection load='1av5' size='340' side='right'caption='[[1av5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AVA:Active+Site+HIS+Responsible+For+Forming+The+Transient+Nu+...'>AVA</scene>, <scene name='pdbsite=AVB:Active+Site+HIS+Responsible+For+Forming+The+Transient+Nu+...'>AVB</scene>, <scene name='pdbsite=HNA:HIS+Triad+For+Which+This+Family+Was+Named'>HNA</scene> and <scene name='pdbsite=HNB:HIS+Triad+For+Which+This+Family+Was+Named'>HNB</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AP2:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>AP2</scene>
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<table><tr><td colspan='2'>[[1av5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AV5 FirstGlance]. <br>
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|ACTIVITY=
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</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>
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|GENE= HPKCI-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=AP2:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>AP2</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1av5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1av5 OCA], [https://pdbe.org/1av5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1av5 RCSB], [https://www.ebi.ac.uk/pdbsum/1av5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1av5 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1av5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1av5 OCA], [http://www.ebi.ac.uk/pdbsum/1av5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1av5 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/HINT1_HUMAN HINT1_HUMAN] Hydrolyzes adenosine 5'-monophosphoramidate substrates such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-acetyl lysine methyl ester and AMP-NH2 (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/av/1av5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1av5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.
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'''PKCI-SUBSTRATE ANALOG'''
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Structure-based analysis of catalysis and substrate definition in the HIT protein family.,Lima CD, Klein MG, Hendrickson WA Science. 1997 Oct 10;278(5336):286-90. PMID:9323207<ref>PMID:9323207</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1av5" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.
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*[[Histidine triad nucleotide-binding protein 3D structures|Histidine triad nucleotide-binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1AV5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AV5 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structure-based analysis of catalysis and substrate definition in the HIT protein family., Lima CD, Klein MG, Hendrickson WA, Science. 1997 Oct 10;278(5336):286-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9323207 9323207]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hendrickson, W A.]]
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[[Category: Hendrickson WA]]
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[[Category: Klein, M G.]]
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[[Category: Klein MG]]
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[[Category: Lima, C D.]]
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[[Category: Lima CD]]
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[[Category: histidine triad protein family]]
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[[Category: hit protein family]]
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[[Category: nucleotidyl hydrolase]]
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[[Category: nucleotidyl transferase]]
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[[Category: pkci-1]]
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[[Category: protein kinase inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:05 2008''
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Current revision

PKCI-SUBSTRATE ANALOG

PDB ID 1av5

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