5ptp: Difference between revisions
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[[Image:5ptp.gif|left|200px]]<br /> | [[Image:5ptp.gif|left|200px]]<br /><applet load="5ptp" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="5ptp" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="5ptp, resolution 1.34Å" /> | caption="5ptp, resolution 1.34Å" /> | ||
'''STRUCTURE OF HYDROLASE (SERINE PROTEINASE)'''<br /> | '''STRUCTURE OF HYDROLASE (SERINE PROTEINASE)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
5PTP 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 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entries 4PTP, 3PTP, 2PTP and 1PTP. 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] | 5PTP 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 as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entries 4PTP, 3PTP, 2PTP and 1PTP. 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] Known structural/functional Sites: <scene name='pdbsite=BIN:Is The Specific Binding Pocket. ASP 189 At The Bottom Of ...'>BIN</scene>, <scene name='pdbsite=CAT:The Catalytic Site. It Is Composed Of Residues ASP 102, ...'>CAT</scene> and <scene name='pdbsite=ION:Contains A Tightly Bound Positive Ion Which Is prob. A C ...'>ION</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5PTP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
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Revision as of 21:37, 18 December 2007
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STRUCTURE OF HYDROLASE (SERINE PROTEINASE)
OverviewOverview
The solvent structure in orthorhombic crystals of bovine trypsin has been, independently determined by X-ray diffraction to 1.35 A resolution and by, neutron diffraction to 2.1 A resolution. A consensus model of the water, molecule positions was obtained using oxygen positions identified in the, electron density map determined by X-ray diffraction, which were verified, by comparison to D2O-H2O difference neutron scattering density. Six of 184, water molecules in the X-ray structure, all with B-factors greater than 50, A2, were found to be spurious after comparison with neutron results., Roughly two-thirds of the water of hydration expected from thermodynamic, data for proteins was localized by neutron diffraction; approximately, one-half of the water of hydration was located by X-ray diffraction. Polar, regions of the protein are well hydrated, and significant D2O-H2O, difference density is seen for a small number of water molecules in a, second shell of hydration. Hydrogen bond lengths and angles calculated, from unconstrained refinement of water positions are distributed about, values typically seen in small molecule structures. Solvent models found, in seven other bovine trypsin and trypsinogen and rat trypsin structures, determined by X-ray diffraction were compared. Internal water molecules, are well conserved in all trypsin structures including anionic rat, trypsin, which is 65% homologous to bovine trypsin. Of the 22 conserved, waters in trypsin, 19 were also found in trypsinogen, suggesting that they, are located in regions of the apoprotein that are structurally conserved, in the transition to the mature protein. Seven waters were displaced upon, activation of trypsinogen. Water structure at crystal contacts is not, generally conserved in different crystal forms. Three groups of integral, structural water molecules are highly conserved in all solvent structures, including a spline of water molecules inserted between two beta-strands, which may resemble an intermediate in the formation of beta sheets during, the folding of a protein.
About this StructureAbout this Structure
5PTP is a Single protein structure of sequence from Bos taurus with CA as ligand. This structure superseeds the now removed PDB entries 4PTP, 3PTP, 2PTP and 1PTP. Active as Trypsin, with EC number 3.4.21.4 Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
ReferenceReference
Solvent structure in crystals of trypsin determined by X-ray and neutron diffraction., Finer-Moore JS, Kossiakoff AA, Hurley JH, Earnest T, Stroud RM, Proteins. 1992 Mar;12(3):203-22. PMID:1557349
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