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.

8tln

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8tln"

Categories: Bacillus thermoproteolyticus | Large Structures | Matthews BW | Tronrud D

@@ Line 1: / Line 1: @@
-[[Image:8tln.gif|left|200px]]
- {{Structure
+==STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS==
-|PDB= 8tln |SIZE=350|CAPTION= <scene name='initialview01'>8tln</scene>, resolution 1.6&Aring;
+<StructureSection load='8tln' size='340' side='right'caption='[[8tln]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+<table><tr><td colspan='2'>[[8tln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3tln 3tln], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tln 1tln] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2tln 2tln]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TLN FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
-|GENE=
+<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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8tln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tln OCA], [https://pdbe.org/8tln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tln RCSB], [https://www.ebi.ac.uk/pdbsum/8tln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tln ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=8tln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tln OCA], [http://www.ebi.ac.uk/pdbsum/8tln PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=8tln RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease.
+== 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/tl/8tln_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=8tln ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS'''
+==See Also==
+*[[Thermolysin 3D structures|Thermolysin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Crystal structures are known for three members of the bacterial neutral protease family: thermolysin from Bacillus thermoproteolyticus (TLN), the neutral protease from Bacillus cereus (NEU), and the elastase of Pseudomonas aeruginosa (PAE), both in free and ligand-bound forms. Each enzyme consists of an N-terminal and C-terminal domain with the active site formed at the junction of the two domains. Comparison of the different molecules reveals that the structure within each domain is well conserved, but there are substantial hinge-bending displacements (up to 16 degrees) of one domain relative to the other. These domain motions can be correlated with the presence or absence of bound inhibitor, as was previously observed in the specific example of PAE [Thayer, M.M., Flaherty, K.M., &amp; McKay, D.B. (1991) J. Biol. Chem. 266, 2864-2871]. The binding of inhibitor appears to be associated with a reduction of the domain hinge-bending angle by 6-14 degrees and a closure of the "jaws" of the active site cleft by about 2 A. Crystallographic refinement of the structure of thermolysin suggests that electron density seen in the active site of the enzyme in the original structure determination probably corresponds to a bound dipeptide. Thus, the crystal structure appears to correspond to an enzyme-inhibitor or enzyme-product complex, rather than the free enzyme, as has previously been assumed.
-==About this Structure==
-TLN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. This structure supersedes the now removed PDB entries 3TLN, 1TLN and 2TLN. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TLN OCA].
-==Reference==
-Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis., Holland DR, Tronrud DE, Pley HW, Flaherty KM, Stark W, Jansonius JN, McKay DB, Matthews BW, Biochemistry. 1992 Nov 24;31(46):11310-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1445869 1445869]
 [[Category: Bacillus thermoproteolyticus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Thermolysin]]
+[[Category: Matthews BW]]
-[[Category: Matthews, B W.]]
+[[Category: Tronrud D]]
-[[Category: Tronrud, D.]]
-[[Category: hydrolase(metalloproteinase)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:45:53 2008''

8tln

From Proteopedia

Current revision

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox