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New page: left|200px<br /><applet load="1fbl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbl, resolution 2.5Å" /> '''STRUCTURE OF FULL-LEN...
 
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[[Image:1fbl.jpg|left|200px]]<br /><applet load="1fbl" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fbl, resolution 2.5&Aring;" />
'''STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER'''<br />


==Overview==
==STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER==
BACKGROUND: The collagenases are members of the family of zinc-dependent, enzymes known as the matrix metalloproteinases (MMPs). They are the only, proteinases that specifically cleave the collagen triple helix, and are, important in a large number of physiological and pathological processes., Structures are known for the N-terminal catalytic' domain of collagenases, MMP-1 and MMP-8 and of stromelysin (MMP-3). This catalytic domain alone, which comprises about 150 amino acids, has no activity against collagen. A, second domain, of 200 amino acids, is homologous to haemopexin, a, haem-binding glycoprotein. RESULTS: The crystal structure of full-length, MMP-1 at 2.5 A resolution gives an R-factor of 21.7%. Two domains are, connected by an exposed proline-rich linker of 17 amino acids, which is, probably flexible and has no secondary structure. The catalytic domain, resembles those previously observed, and contains three calcium-binding, sites. The haemopexin-like domain contains four units of four-stranded, antiparallel beta sheet stabilized on its fourfold axis by a cation, which, is probably calcium. The domain constitutes a four-bladed beta-propeller, structure in which the blades are scarcely twisted. CONCLUSIONS: The, exposed linker accounts for the difficulty in purifying full-length, collagenase. The C-terminal domain provides a structural model for, haemopexin and its homologues. It controls the specificity of MMPs, affecting both substrate and inhibitor binding, although its role remains, obscure. These structural results should aid the design of site-specific, mutants which will reveal further details of the specificity mechanism.
<StructureSection load='1fbl' size='340' side='right'caption='[[1fbl]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fbl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBL 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=HTA:N-[3-(N-HYDROXYCARBOXAMIDO)-2-(2-METHYLPROPYL)-PROPANOYL]-O-TYROSINE-N-METHYLAMIDE'>HTA</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=1fbl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbl OCA], [https://pdbe.org/1fbl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fbl RCSB], [https://www.ebi.ac.uk/pdbsum/1fbl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fbl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MMP1_PIG MMP1_PIG] Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X.
== 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/fb/1fbl_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=1fbl ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FBL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with CA, ZN and HTA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Interstitial_collagenase Interstitial collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.7 3.4.24.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FBL OCA].
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller., Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE, et al., Structure. 1995 Jun 15;3(6):541-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8590015 8590015]
[[Category: Large Structures]]
[[Category: Interstitial collagenase]]
[[Category: Single protein]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Blow, D.M.]]
[[Category: Blow DM]]
[[Category: Brick, P.]]
[[Category: Brick P]]
[[Category: Li, J.]]
[[Category: Li J]]
[[Category: CA]]
[[Category: HTA]]
[[Category: ZN]]
[[Category: metalloprotease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:47:38 2007''

Latest revision as of 10:13, 20 March 2024

STRUCTURE OF FULL-LENGTH PORCINE SYNOVIAL COLLAGENASE (MMP1) REVEALS A C-TERMINAL DOMAIN CONTAINING A CALCIUM-LINKED, FOUR-BLADED BETA-PROPELLER

1fbl, resolution 2.50Å

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