2dso
From Proteopedia
(New page: 200px<br /><applet load="2dso" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dso, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:2dso.gif|left|200px]]<br /><applet load="2dso" size=" | + | [[Image:2dso.gif|left|200px]]<br /><applet load="2dso" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dso, resolution 2.10Å" /> | caption="2dso, resolution 2.10Å" /> | ||
'''Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''<br /> | '''Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Drp35 is a protein induced by cell wall-affecting antibiotics or | + | 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 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 CA and GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: beta propeller]] | [[Category: beta propeller]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:12 2008'' |
Revision as of 15:02, 21 February 2008
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Crystal structure of D138N mutant of Drp35, a 35kDa drug responsive protein from Staphylococcus aureus
Overview
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 Structure
2DSO is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Active as 1,4-lactonase, with EC number 3.1.1.25 Full crystallographic information is available from OCA.
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:17166853
Page seeded by OCA on Thu Feb 21 17:02:12 2008
Categories: 1,4-lactonase | Single protein | Staphylococcus aureus | Morikawa, K. | Ohki, Y. | Ohta, T. | Tanaka, I. | Tanaka, Y. | Watanabe, N. | Yao, M. | CA | GOL | Beta propeller
