1k23
From Proteopedia
(New page: 200px<br /><applet load="1k23" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k23, resolution 3.00Å" /> '''Inorganic Pyrophosph...) |
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| - | [[Image:1k23.jpg|left|200px]]<br /><applet load="1k23" size=" | + | [[Image:1k23.jpg|left|200px]]<br /><applet load="1k23" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k23, resolution 3.00Å" /> | caption="1k23, resolution 3.00Å" /> | ||
'''Inorganic Pyrophosphatase (Family II) from Bacillus subtilis'''<br /> | '''Inorganic Pyrophosphatase (Family II) from Bacillus subtilis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recently, a new class of soluble inorganic pyrophosphatase (type-C PPase) | + | Recently, a new class of soluble inorganic pyrophosphatase (type-C PPase) has been described that is not homologous in amino acid sequence or kinetic properties to the well-studied PPases (types A and B) found in many organisms from bacteria to humans and thought to be essential to the cell. Structural studies of the type-C PPases from Streptococcus gordonii and Bacillus subtilis reveal a homodimeric structure, with each polypeptide folding into two domains joined by a flexible hinge. The active site, formed at the interface between the N and C-terminal domains, binds two manganese ions approximately 3.6 A apart in a conformation resembling binuclear metal centres found in other hydrolytic enzymes. An activated water molecule bridging the two metal ions is likely poised for nucleophilic attack of the substrate. Importantly, the S. gordonii and B. subtilis enzymes have crystallised in strikingly different conformations. In both subunits of the S. gordonii crystal structure (1.5 A resolution) the C-terminal domain is positioned such that the active site is occluded, with a sulphate ion bound in the active site. In contrast, in the B. subtilis structure (3.0 A resolution) the C-terminal domain is rotated by about 90 degrees, leaving the active site wide open and accessible for substrate binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1K23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http:// | + | 1K23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K23 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ilias, M.]] | [[Category: Ilias, M.]] | ||
[[Category: Konopka, M.]] | [[Category: Konopka, M.]] | ||
| - | [[Category: Milner, A | + | [[Category: Milner, A J.]] |
| - | [[Category: White, S | + | [[Category: White, S A.]] |
| - | [[Category: Young, T | + | [[Category: Young, T W.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: binuclear metal centre]] | [[Category: binuclear metal centre]] | ||
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[[Category: manganese]] | [[Category: manganese]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:14 2008'' |
Revision as of 11:29, 21 February 2008
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Inorganic Pyrophosphatase (Family II) from Bacillus subtilis
Overview
Recently, a new class of soluble inorganic pyrophosphatase (type-C PPase) has been described that is not homologous in amino acid sequence or kinetic properties to the well-studied PPases (types A and B) found in many organisms from bacteria to humans and thought to be essential to the cell. Structural studies of the type-C PPases from Streptococcus gordonii and Bacillus subtilis reveal a homodimeric structure, with each polypeptide folding into two domains joined by a flexible hinge. The active site, formed at the interface between the N and C-terminal domains, binds two manganese ions approximately 3.6 A apart in a conformation resembling binuclear metal centres found in other hydrolytic enzymes. An activated water molecule bridging the two metal ions is likely poised for nucleophilic attack of the substrate. Importantly, the S. gordonii and B. subtilis enzymes have crystallised in strikingly different conformations. In both subunits of the S. gordonii crystal structure (1.5 A resolution) the C-terminal domain is positioned such that the active site is occluded, with a sulphate ion bound in the active site. In contrast, in the B. subtilis structure (3.0 A resolution) the C-terminal domain is rotated by about 90 degrees, leaving the active site wide open and accessible for substrate binding.
About this Structure
1K23 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.
Reference
The "open" and "closed" structures of the type-C inorganic pyrophosphatases from Bacillus subtilis and Streptococcus gordonii., Ahn S, Milner AJ, Futterer K, Konopka M, Ilias M, Young TW, White SA, J Mol Biol. 2001 Nov 2;313(4):797-811. PMID:11697905
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