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1hpg

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[[Image:1hpg.gif|left|200px]]
 
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{{Structure
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==A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding==
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|PDB= 1hpg |SIZE=350|CAPTION= <scene name='initialview01'>1hpg</scene>, resolution 1.5&Aring;
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<StructureSection load='1hpg' size='340' side='right'caption='[[1hpg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</scene>
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<table><tr><td colspan='2'>[[1hpg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HPG FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamyl_endopeptidase_II Glutamyl endopeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.82 3.4.21.82] </span>
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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]] 1.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOC:TERT-BUTYL+HYDROGEN+CARBONATE'>BOC</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=1hpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpg OCA], [https://pdbe.org/1hpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hpg RCSB], [https://www.ebi.ac.uk/pdbsum/1hpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hpg 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=1hpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpg OCA], [http://www.ebi.ac.uk/pdbsum/1hpg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hpg RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/GLUP_STRGR GLUP_STRGR] Preferentially cleaves peptide bonds on the carboxyl-terminal side of glutamate.
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== Evolutionary Conservation ==
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'''A GLUTAMIC ACID SPECIFIC SERINE PROTEASE UTILIZES A NOVEL HISTIDINE TRIAD IN SUBSTRATE BINDING'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/1hpg_consurf.spt"</scriptWhenChecked>
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Proteases specific for cleavage after acidic residues have been implicated in several disease states, including epidermolysis, inflammation, and viral processing. A serine protease with specificity toward glutamic acid substrates (Glu-SGP) has been crystallized in the presence of a tetrapeptide ligand and its structure determined and refined to an R-factor of 17% at 2.0-A resolution. This structure provides an initial description of the design of proteolytic specificity for negatively charged residues. While the overall fold of Glu-SGP closely resembles that observed in the pancreatic-type serine proteases, stabilization of the negatively charged substrate when bound to this protein appears to involve a more extensive part of the protease than previously observed. The substrate carboxylate is bound to a histidine side chain, His213, which provides the primary electrostatic compensation of the negative charge on the substrate, and to two serine hydroxyls, Ser192 and Ser216. Glu-SGP displays maximum activity at pH 8.3, and assuming normal pKa's, the glutamate side chain and His213 will be negatively charged and neutral, respectively, at this pH. In order for His213 to carry a positive charge at the optimal pH, its pKa will have to be raised by at least two units. An alternative mechanism for substrate charge compensation is suggested that involves a novel histidine triad, His213, His199, and His228, not observed in any other serine protease. The C-terminal alpha-helix, ubiquitous to all pancreatic-type proteases, is directly linked to this histidine triad and may also play a role in substrate stabilization.(ABSTRACT TRUNCATED AT 250 WORDS)
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1HPG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPG OCA].
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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=1hpg ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding., Nienaber VL, Breddam K, Birktoft JJ, Biochemistry. 1993 Nov 2;32(43):11469-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8105890 8105890]
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</StructureSection>
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[[Category: Glutamyl endopeptidase II]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Streptomyces griseus]]
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[[Category: Birktoft, J J.]]
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[[Category: Birktoft JJ]]
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[[Category: Nienaber, V L.]]
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[[Category: Nienaber VL]]
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[[Category: hydrolase (serine protease)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:38 2008''
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Current revision

A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding

PDB ID 1hpg

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