2dso: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:2dso.gif|left|200px]]<br /><applet load="2dso" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2dso.gif|left|200px]]
caption="2dso, resolution 2.10&Aring;" />
 
'''Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''<br />
{{Structure
|PDB= 2dso |SIZE=350|CAPTION= <scene name='initialview01'>2dso</scene>, resolution 2.10&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/1,4-lactonase 1,4-lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.25 3.1.1.25]
|GENE=
}}
 
'''Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
2DSO 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/1,4-lactonase 1,4-lactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.25 3.1.1.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DSO OCA].  
2DSO 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=2DSO OCA].  


==Reference==
==Reference==
Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity., Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I, J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17166853 17166853]
Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity., Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I, J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17166853 17166853]
[[Category: 1,4-lactonase]]
[[Category: 1,4-lactonase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 25: Line 34:
[[Category: beta propeller]]
[[Category: beta propeller]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:12 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:31:01 2008''

Revision as of 17:31, 20 March 2008

File:2dso.gif


PDB ID 2dso

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: and
Activity: 1,4-lactonase, with EC number 3.1.1.25
Coordinates: save as pdb, mmCIF, xml



Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus


OverviewOverview

Drp35 is a protein induced by cell wall-affecting antibiotics or detergents; it possesses calcium-dependent lactonase activity. To determine the molecular basis of the lactonase activity, we first solved the crystal structures of Drp35 with and without Ca(2+); these showed that the molecule has a six-bladed beta-propeller structure with two calcium ions bound at the center of the beta-propeller and surface region. Mutational analyses of evolutionarily conserved residues revealed that the central calcium-binding site is essential for the enzymatic activity of Drp35. Substitution of some other amino acid residues for the calcium-binding residues demonstrated the critical contributions of Glu(48), Asp(138), and Asp(236) to the enzymatic activity. Differential scanning calorimetric analysis revealed that the loss of activity of E48Q and D236N, but not D138N, was attributed to their inability to hold the calcium ion. Further structural analysis of the D138N mutant indicates that it lacks a water molecule bound to the calcium ion rather than the calcium ion itself. Based on these observations and structural information, a possible catalytic mechanism in which the calcium ion and its binding residues play direct roles was proposed for the lactonase activity of Drp35.

About this StructureAbout this Structure

2DSO is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity., Tanaka Y, Morikawa K, Ohki Y, Yao M, Tsumoto K, Watanabe N, Ohta T, Tanaka I, J Biol Chem. 2007 Feb 23;282(8):5770-80. Epub 2006 Dec 13. PMID:17166853

Page seeded by OCA on Thu Mar 20 16:31:01 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA