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1jan

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COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (PHE79 FORM)

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Retrieved from "http://52.214.119.220/wiki/index.php/1jan"

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-[[Image:1jan.gif|left|200px]]<br />
-<applet load="1jan" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1jan, resolution 2.5&Aring;" />
-'''COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (PHE79 FORM)'''<br />
-==Overview==
+==COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (PHE79 FORM)==
-For the collagenases PMNL-CL and FIB-CL, the presence of the N-terminal, Phe79 correlates with an increase in proteolytic activity. We have, determined the X-ray crystal structure of the recombinant Phe79-Gly242, catalytic domain of human neutrophil collagenase (PMNL-CL, MMP-8) using, the recently solved model of the Met80-Gly242 form for phasing and, subsequently refined it to a final crystallographic R-factor of 18.0% at, 2.5 A resolution. The PMNL-CL catalytic domain is a spherical molecule, with a flat active site cleft separating a smaller C-terminal subdomain, from a bigger N-terminal domain, that harbours two zinc ions, namely a, 'structural' and a 'catalytic' zinc, and two calcium ions. The N-terminal, segment prior to Pro86, which is disordered in the Met80-Gly242 form, packs against a concave hydrophobic surface made by the C-terminal helix., The N-terminal Phe79 ammonium group makes a salt link with the side chain, carboxylate group of the strictly conserved Asp232. Stabilization of the, catalytic site might be conferred via strong hydrogen bonds made by the, adjacent, likewise strictly conserved Asp233 with the characteristic, 'Met-turn', which forms the base of the active site residues.
+<StructureSection load='1jan' size='340' side='right'caption='[[1jan]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1jan]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JAN 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]] 2.5&#8491;</td></tr>
+<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=HOA:HYDROXYAMINE'>HOA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1jan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jan OCA], [https://pdbe.org/1jan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jan RCSB], [https://www.ebi.ac.uk/pdbsum/1jan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jan ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MMP8_HUMAN MMP8_HUMAN] Can degrade fibrillar type I, II, and III collagens.
+== 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/ja/1jan_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=1jan ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-JAN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, ZN and HOA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JAN OCA].
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study., Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Piper M, Tschesche H, Bode W, FEBS Lett. 1994 Jan 31;338(2):227-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8307185 8307185]
 [[Category: Homo sapiens]]
-[[Category: Neutrophil collagenase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Bode W]]
-[[Category: Bode, W.]]
+[[Category: Grams F]]
-[[Category: Grams, F.]]
+[[Category: Huber R]]
-[[Category: Huber, R.]]
+[[Category: Kleine T]]
-[[Category: Kleine, T.]]
+[[Category: Pieper M]]
-[[Category: Pieper, M.]]
+[[Category: Reinemer P]]
-[[Category: Reinemer, P.]]
+[[Category: Schnierer S]]
-[[Category: Schnierer, S.]]
+[[Category: Tschesche H]]
-[[Category: Tschesche, H.]]
-[[Category: CA]]
-[[Category: HOA]]
-[[Category: ZN]]
-[[Category: metalloprotease]]
-[[Category: metzincins]]
-[[Category: zinc-endopeptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:39:01 2007''

1jan

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Current revision

COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (PHE79 FORM)

Structural highlights

Function

Evolutionary Conservation

See Also

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