1enc

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[[Image:1enc.jpg|left|200px]]<br /><applet load="1enc" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1enc.jpg|left|200px]]
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caption="1enc, resolution 1.95&Aring;" />
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'''CRYSTAL STRUCTURES OF THE BINARY CA2+ AND PDTP COMPLEXES AND THE TERNARY COMPLEX OF THE ASP 21->GLU MUTANT OF STAPHYLOCOCCAL NUCLEASE. IMPLICATIONS FOR CATALYSIS AND LIGAND BINDING'''<br />
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{{Structure
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|PDB= 1enc |SIZE=350|CAPTION= <scene name='initialview01'>1enc</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=THP:THYMIDINE-3',5'-DIPHOSPHATE'>THP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1]
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|GENE=
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}}
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'''CRYSTAL STRUCTURES OF THE BINARY CA2+ AND PDTP COMPLEXES AND THE TERNARY COMPLEX OF THE ASP 21->GLU MUTANT OF STAPHYLOCOCCAL NUCLEASE. IMPLICATIONS FOR CATALYSIS AND LIGAND BINDING'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ENC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=THP:'>THP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENC OCA].
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1ENC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ENC OCA].
==Reference==
==Reference==
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Crystal structures of the binary Ca2+ and pdTp complexes and the ternary complex of the Asp21--&gt;Glu mutant of staphylococcal nuclease. Implications for catalysis and ligand binding., Libson AM, Gittis AG, Lattman EE, Biochemistry. 1994 Jul 5;33(26):8007-16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8025105 8025105]
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Crystal structures of the binary Ca2+ and pdTp complexes and the ternary complex of the Asp21--&gt;Glu mutant of staphylococcal nuclease. Implications for catalysis and ligand binding., Libson AM, Gittis AG, Lattman EE, Biochemistry. 1994 Jul 5;33(26):8007-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8025105 8025105]
[[Category: Micrococcal nuclease]]
[[Category: Micrococcal nuclease]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase(phosphoric diester)]]
[[Category: hydrolase(phosphoric diester)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:57:52 2008''

Revision as of 08:57, 20 March 2008


PDB ID 1enc

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands: and
Activity: Micrococcal nuclease, with EC number 3.1.31.1
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURES OF THE BINARY CA2+ AND PDTP COMPLEXES AND THE TERNARY COMPLEX OF THE ASP 21->GLU MUTANT OF STAPHYLOCOCCAL NUCLEASE. IMPLICATIONS FOR CATALYSIS AND LIGAND BINDING


Overview

The crystal structure of the Asp21-->Glu mutant (D21E) of staphylococcal nuclease (SNase) has been determined in three different complex forms. The structure of the D21E ternary complex in which D21E is bound to both Ca2+ and the transition-state analogue, thymidine 3',5'-diphosphate (pdTp), was determined to 1.95-A resolution. The structures of both binary complexes, D21E bound either to Ca2+ or pdTp, were determined to 2.15- and 2.05-A resolution, respectively. In the ternary structure, we find a 1.5-A movement of the Ca2+ in the active site, evidence of bidentate coordination of Ca2+ by Glu21 and inner-sphere coordination of the Ca2+ by Glu43. Comparison of the D21E binary structures with the ternary model shows large movements of active site side chains expected to play a direct role in catalysis. Glu43 moves in the binary nucleotide complex, whereas Arg35 is oriented differently in the binary metal complex. From these changes, we seek to explain the basis for the 1500-fold decrease in Vmax of D21E relative to wild-type SNase (WT). Furthermore, we describe direct structural evidence which explains the cooperativity of Ca2+ and pdTp binding in the ternary complex relative to that of the binary complexes.

About this Structure

1ENC is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Crystal structures of the binary Ca2+ and pdTp complexes and the ternary complex of the Asp21-->Glu mutant of staphylococcal nuclease. Implications for catalysis and ligand binding., Libson AM, Gittis AG, Lattman EE, Biochemistry. 1994 Jul 5;33(26):8007-16. PMID:8025105

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