1slv: Difference between revisions

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[[Image:1slv.gif|left|200px]]<br /><applet load="1slv" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1slv.gif|left|200px]]
caption="1slv, resolution 2.3&Aring;" />
 
'''RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND'''<br />
{{Structure
|PDB= 1slv |SIZE=350|CAPTION= <scene name='initialview01'>1slv</scene>, resolution 2.3&Aring;
|SITE= <scene name='pdbsite=CU1:Cu+Binding+Site'>CU1</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
|ACTIVITY= [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]
|GENE= RAT ANIONIC TRYPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), RAT ANIONIC TRYPSIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
}}
 
'''RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; COPPER-BOUND'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=CU:'>CU</scene> 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] Known structural/functional Site: <scene name='pdbsite=CU1:Cu+Binding+Site'>CU1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLV OCA].  
1SLV is a [[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]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SLV OCA].  


==Reference==
==Reference==
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]
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://www.ncbi.nlm.nih.gov/pubmed/8634241 8634241]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: complex]]
[[Category: complex]]
[[Category: inhibitor]]
[[Category: inhibitor]]
[[Category: metal binding sites]]
[[Category: metal binding site]]
[[Category: metalloproteins]]
[[Category: metalloprotein]]
[[Category: protease-substrate interactions]]
[[Category: protease-substrate interaction]]
[[Category: protein engineering]]
[[Category: protein engineering]]
[[Category: serine protease]]
[[Category: serine protease]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:49 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:38 2008''

Revision as of 15:06, 20 March 2008

File:1slv.gif


PDB ID 1slv

Drag the structure with the mouse to rotate
, resolution 2.3Å
Sites:
Ligands: , and
Gene: RAT ANIONIC TRYPSIN (Escherichia coli), RAT ANIONIC TRYPSIN (Rattus norvegicus)
Activity: Trypsin, with EC number 3.4.21.4
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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 kinetics of the metal-regulated catalysis. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins.

About this StructureAbout this Structure

1SLV is a Protein complex structure of sequences from Escherichia coli and Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

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:8634241

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