1tlx: Difference between revisions

Revision as of 16:15, 21 February 2008

THERMOLYSIN (NATIVE)

OverviewOverview

Multiple-solvent crystal structure determination (MSCS) allows the position and orientation of bound solvent fragments to be identified by determining the structure of protein crystals soaked in organic solvents. We have extended this technique by the determination of high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 2% to 100% isopropanol. The procedure causes only minor changes to the conformation of the protein, and an increasing number of isopropanol interaction sites could be identified as the solvent concentration is increased. Isopropanol occupies all four of the main subsites in the active site, although this was only observed at very high concentrations of isopropanol for three of the four subsites. Analysis of the isopropanol positions shows little correlation with interaction energy computed using a molecular mechanics force field, but the experimentally determined positions of isopropanol are consistent with the structures of known protein-ligand complexes of TLN.

About this StructureAbout this Structure

1TLX is a Single protein structure of sequence from Bacillus thermoproteolyticus with , and as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.

ReferenceReference

Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol., English AC, Done SH, Caves LS, Groom CR, Hubbard RE, Proteins. 1999 Dec 1;37(4):628-40. PMID:10651278

Page seeded by OCA on Thu Feb 21 15:14:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1tlx.jpg|left|200px]]<br /><applet load="1tlx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tlx.jpg|left|200px]]<br /><applet load="1tlx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tlx, resolution 2.10&Aring;" />
 '''THERMOLYSIN (NATIVE)'''<br />
 ==Overview==
-Multiple-solvent crystal structure determination (MSCS) allows the, position and orientation of bound solvent fragments to be identified by, determining the structure of protein crystals soaked in organic solvents., We have extended this technique by the determination of high-resolution, crystal structures of thermolysin (TLN), generated from crystals soaked in, 2% to 100% isopropanol. The procedure causes only minor changes to the, conformation of the protein, and an increasing number of isopropanol, interaction sites could be identified as the solvent concentration is, increased. Isopropanol occupies all four of the main subsites in the, active site, although this was only observed at very high concentrations, of isopropanol for three of the four subsites. Analysis of the isopropanol, positions shows little correlation with interaction energy computed using, a molecular mechanics force field, but the experimentally determined, positions of isopropanol are consistent with the structures of known, protein-ligand complexes of TLN.
+Multiple-solvent crystal structure determination (MSCS) allows the position and orientation of bound solvent fragments to be identified by determining the structure of protein crystals soaked in organic solvents. We have extended this technique by the determination of high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 2% to 100% isopropanol. The procedure causes only minor changes to the conformation of the protein, and an increasing number of isopropanol interaction sites could be identified as the solvent concentration is increased. Isopropanol occupies all four of the main subsites in the active site, although this was only observed at very high concentrations of isopropanol for three of the four subsites. Analysis of the isopropanol positions shows little correlation with interaction energy computed using a molecular mechanics force field, but the experimentally determined positions of isopropanol are consistent with the structures of known protein-ligand complexes of TLN.
 ==About this Structure==
-TLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] with ZN, CA and DMS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TLX OCA].
+TLX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DMS:'>DMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TLX OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Thermolysin]]
-[[Category: Done, S.H.]]
+[[Category: Done, S H.]]
-[[Category: English, A.C.]]
+[[Category: English, A C.]]
-[[Category: Groom, C.R.]]
+[[Category: Groom, C R.]]
-[[Category: Hubbard, R.E.]]
+[[Category: Hubbard, R E.]]
 [[Category: CA]]
 [[Category: DMS]]
@@ Line 25: / Line 25: @@
 [[Category: organic solvent]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:23:40 2007''
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