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1tld

From Proteopedia

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(New page: 200px<br /><applet load="1tld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tld, resolution 1.5&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1tld.gif|left|200px]]<br /><applet load="1tld" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tld, resolution 1.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.5 ANGSTROMS RESOLUTION IN A CRYSTAL FORM WITH LOW MOLECULAR PACKING DENSITY. ACTIVE SITE GEOMETRY, ION PAIRS AND SOLVENT STRUCTURE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.5 ANGSTROMS RESOLUTION IN A CRYSTAL FORM WITH LOW MOLECULAR PACKING DENSITY. ACTIVE SITE GEOMETRY, ION PAIRS AND SOLVENT STRUCTURE==
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The crystal structure of bovine pancreatic beta-trypsin (BPT) has been, determined from a novel orthorhombic crystal form which contains, substantially more solvent (filling 57% of the volume of the unit cell), than previously determined orthorhombic (44%) and trigonal (37%) BPT, structures. The native and benzamidine-inhibited crystal structures of BPT, in ammonium sulphate at pH 5.3 have been determined for the new form by, molecular replacement techniques. The structures have been refined at 1.5, A resolution with final R-values of 16.7% and 16.9%, respectively., Comparison with the previously refined old orthorhombic forms shows that, the overall conformation of the protein backbone is highly conserved. A, great number of previously undefined side-chains have been located in, density. At the C terminus an extra ion pair involving lysines 87 and 107, has been revealed. A far more detailed picture of the ordered solvent, structure has been derived. Thirty water clusters have been identified. A, large water network extends from the calcium binding site to the, activation area and the autolysis loop. There is evidence for a water, channel reaching from the depth of the specificity pocket to the nearby, protein surface which might be involved in the displacement of water, molecules upon substrate binding. A sulphate anion which forms hydrogen, bonds to the active site residues His57, Ser195 and Gly193 was for the, first time positioned in clearly defined electron density. Interaction, with the sulphate ion may explain the increase in the pKa value of His57, at high sulphate concentrations which was observed by nuclear magnetic, resonance studies of a bacterial serine protease both in crystalline form, and in solution. Thus, a His-Ser hydrogen bond will not exist in solvents, containing sulphate at low pH (up to at least 6.8) where the imidazole of, His57 is protonated. The new crystal form is of considerable interest for, substrate binding studies. Wide solvent channels should allow diffusion of, large substrates (comparable in size to, e.g. pancreatic trypsin, inhibitor) into the enzyme crystal. The active site is accessible;, intermolecular contact areas are further remote from the active site than, in the old orthorhombic form.
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<StructureSection load='1tld' size='340' side='right'caption='[[1tld]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TLD FirstGlance]. <br>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1tld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tld OCA], [https://pdbe.org/1tld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tld RCSB], [https://www.ebi.ac.uk/pdbsum/1tld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tld ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
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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/tl/1tld_consurf.spt"</scriptWhenChecked>
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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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</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=1tld ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TLD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLD OCA].
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of bovine beta-trypsin at 1.5 A resolution in a crystal form with low molecular packing density. Active site geometry, ion pairs and solvent structure., Bartunik HD, Summers LJ, Bartsch HH, J Mol Biol. 1989 Dec 20;210(4):813-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2614845 2614845]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Trypsin]]
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[[Category: Bartsch HH]]
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[[Category: Bartsch, H.H.]]
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[[Category: Bartunik HD]]
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[[Category: Bartunik, H.D.]]
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[[Category: Summers LJ]]
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[[Category: Summers, L.J.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:22:36 2007''
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Current revision

CRYSTAL STRUCTURE OF BOVINE BETA-TRYPSIN AT 1.5 ANGSTROMS RESOLUTION IN A CRYSTAL FORM WITH LOW MOLECULAR PACKING DENSITY. ACTIVE SITE GEOMETRY, ION PAIRS AND SOLVENT STRUCTURE

PDB ID 1tld

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