This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dlk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1dlk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlk, resolution 2.14&Aring;" /> '''CRYSTAL STRUCTURE AN...)
Current revision (09:51, 20 March 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dlk.gif|left|200px]]<br /><applet load="1dlk" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1dlk, resolution 2.14&Aring;" />
 
-
'''CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR==
-
Chymotrypsin is a member of the trypsin family of serine proteases and is, one of the first proteins successfully studied by X-ray crystallography., It is secreted into the intestine as the inactive precursor, chymotrypsinogen; four sequential cleavages of the peptide bonds following, residues 13, 15, 146 and 148 occur to generate the active pi, delta, kappa, and alpha forms of chymotrypsin. (13)C NMR has shown [O'Connell &amp;, Malthouse (1995). Biochem. J. 307, 353-359] that when the delta form of, chymotrypsin is inhibited by 2-(13)C-enriched, benzyloxycarbonylglycylglycylphenylalanyl chloromethane, a tetrahedral, adduct is formed which is thought to be analogous to the tetrahedral, intermediate formed during catalysis. This inhibitor complex has been, crystallized as a dimer in space group P4(1)2(1)2. The structure has been, refined at 2.14 A resolution to an R value of 21.2% (free R = 25.2%)., Conformational differences between delta-chymotrypsin and chymotrypsinogen, in the region of the flexible autolysis loop (residues 145-150) were, observed. This is the first crystal structure of delta-chymotrypsin and, includes two residues which are disordered in previous crystal structures, of active chymotrypsin. A difference of 11.3 A(2) between the average B, values of the monomers within the asymmetric unit is caused by, lattice-disordering effects approximating to rotation of the molecules, about a crystallographic screw axis. The substrate-binding mode of the, inhibitor was similar to other chymotrypsin peptidyl inhibitor complexes, but this is the first published chymotrypsin structure in which the, tetrahedral chloromethyl ketone transition-state analogue is observed., This structure is compared with that of a similar tetrahedral, transition-state analogue which does not alkylate the active-site, histidine residue.
+
<StructureSection load='1dlk' size='340' side='right'caption='[[1dlk]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1dlk]] is a 6 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=1DLK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLK FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HPH:(2S)-2-AMINO-3-PHENYLPROPANE-1,1-DIOL'>HPH</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dlk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dlk OCA], [https://pdbe.org/1dlk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dlk RCSB], [https://www.ebi.ac.uk/pdbsum/1dlk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dlk ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CTRA_BOVIN CTRA_BOVIN]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dl/1dlk_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1dlk ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1DLK 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 CL, GLY and BGG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DLK OCA].
+
*[[Thrombin 3D Structures|Thrombin 3D Structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Crystal structure of delta-chymotrypsin bound to a peptidyl chloromethyl ketone inhibitor., Mac Sweeney A, Birrane G, Walsh MA, O'Connell T, Malthouse JP, Higgins TM, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):280-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10713514 10713514]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Chymotrypsin]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Birrane G]]
-
[[Category: Birrane, G.]]
+
[[Category: Mac Sweeney A]]
-
[[Category: Connell, T.O.]]
+
[[Category: Malthouse JPG]]
-
[[Category: Malthouse, J.P.G.]]
+
[[Category: O'Connell T]]
-
[[Category: Sweeney, A.Mac.]]
+
[[Category: Walsh MA]]
-
[[Category: Walsh, M.A.]]
+
-
[[Category: BGG]]
+
-
[[Category: CL]]
+
-
[[Category: GLY]]
+
-
[[Category: chloromethyl ketone]]
+
-
[[Category: delta-chymotrypsin]]
+
-
[[Category: peptidic inhibior]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:23:18 2007''
+

Current revision

CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR

PDB ID 1dlk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dlk"
Personal tools