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[[Image:1slv.gif|left|200px]]<br />
<applet load="1slv" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1slv, resolution 2.3&Aring;" />
'''RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND'''<br />


==Overview==
==RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND==
The three-dimensional structures of complexes of trypsin N143H, E151H, bound to ecotin A86H are determined at 2.0 A resolution via X-ray, crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for these transition metals was, constructed by substitution of key amino acids with histidine at the, trypsin-ecotin interface in the S2'/P2' pocket. Three histidine side, chains, two on trypsin at positions 143 and 151 and one on ecotin at, position 86, anchor the metals and provide extended catalytic recognition, for substrates with His in the P2' pocket. Comparisons of the, three-dimensional structures show the different geometries that result, upon the binding of metal in the engineered tridentate site and suggest a, structural basis for the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8634241 (full description)]]
<StructureSection load='1slv' size='340' side='right'caption='[[1slv]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1slv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SLV 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=1slv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1slv OCA], [https://pdbe.org/1slv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1slv RCSB], [https://www.ebi.ac.uk/pdbsum/1slv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1slv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ECOT_ECOLI ECOT_ECOLI] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]
== 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/sl/1slv_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=1slv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SLV is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] and [[http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]] with CA, ACT and CU as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Trypsin Trypsin]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4]]. Structure known Active Site: CU1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SLV OCA]].
*[[Ecotin|Ecotin]]
 
*[[Trypsin 3D structures|Trypsin 3D structures]]
==Reference==
__TOC__
X-ray structures of a designed binding site in trypsin show metal-dependent geometry., Brinen LS, Willett WS, Craik CS, Fletterick RJ, Biochemistry. 1996 May 14;35(19):5999-6009. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8634241 8634241]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Trypsin]]
[[Category: Brinen LS]]
[[Category: Brinen, L.S.]]
[[Category: Fletterick RJ]]
[[Category: Fletterick, R.J.]]
[[Category: ACT]]
[[Category: CA]]
[[Category: CU]]
[[Category: complex]]
[[Category: inhibitor]]
[[Category: metal binding sites]]
[[Category: metalloproteins]]
[[Category: protease-substrate interactions]]
[[Category: protein engineering]]
[[Category: serine protease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:04:27 2007''

Latest revision as of 11:33, 1 May 2024

RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUNDRAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND

Structural highlights

1slv is a 2 chain structure with sequence from Escherichia coli and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ECOT_ECOLI General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1slv, resolution 2.30Å

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