1m35: Difference between revisions

Revision as of 14:51, 21 February 2008

Aminopeptidase P from Escherichia coli

OverviewOverview

Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of AMPP has been solved and refined in the orthorhombic space group C222(1) at 2.4 A resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and R(free) = 0.215. The molecular structure confirms most of the previously reported features, including the subunit-subunit interfaces in the tetramer and persistent disorder at some residues. The metal-ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate.

About this StructureAbout this Structure

1M35 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Full crystallographic information is available from OCA.

ReferenceReference

An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution., Graham SC, Lee M, Freeman HC, Guss JM, Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:12777807

Page seeded by OCA on Thu Feb 21 13:50:58 2008

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OCA

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-[[Image:1m35.gif|left|200px]]<br /><applet load="1m35" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1m35.gif|left|200px]]<br /><applet load="1m35" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1m35, resolution 2.40&Aring;" />
 '''Aminopeptidase P from Escherichia coli'''<br />
 ==Overview==
-Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal, residue from an oligopeptide if the second residue is proline. The active, site contains a dinuclear metal centre. Following earlier structural, analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of, AMPP has been solved and refined in the orthorhombic space group C222(1), at 2.4 A resolution. There are six subunits in the asymmetric unit. These, are arranged in two types of tetramer. One tetramer comprises four, crystallographically independent subunits, while the other comprises two, pairs of subunits related by a crystallographic twofold axis. The final, model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms, refined to residuals R = 0.195 and R(free) = 0.215. The molecular, structure confirms most of the previously reported features, including the, subunit-subunit interfaces in the tetramer and persistent disorder at some, residues. The metal-ligand bond lengths at the active site suggest that, one of the two Mn atoms is five-coordinate rather than six-coordinate.
+Aminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of AMPP has been solved and refined in the orthorhombic space group C222(1) at 2.4 A resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and R(free) = 0.215. The molecular structure confirms most of the previously reported features, including the subunit-subunit interfaces in the tetramer and persistent disorder at some residues. The metal-ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate.
 ==About this Structure==
-M35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M35 OCA].
+M35 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M35 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Xaa-Pro aminopeptidase]]
-[[Category: Freeman, H.C.]]
+[[Category: Freeman, H C.]]
-[[Category: Graham, S.C.]]
+[[Category: Graham, S C.]]
-[[Category: Guss, J.M.]]
+[[Category: Guss, J M.]]
 [[Category: Lee, M.]]
 [[Category: MN]]
@@ Line 23: / Line 23: @@
 [[Category: proline specific]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:06:35 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:58 2008''