1apa: Difference between revisions

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[[Image:1apa.gif|left|200px]]<br /><applet load="1apa" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1apa.gif|left|200px]]<br /><applet load="1apa" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1apa, resolution 2.3Å" />

'''X-RAY STRUCTURE OF A POKEWEED ANTIVIRAL PROTEIN, CODED BY A NEW GENOMIC CLONE, AT 0.23 NM RESOLUTION. A MODEL STRUCTURE PROVIDES A SUITABLE ELECTROSTATIC FIELD FOR SUBSTRATE BINDING.'''<br />

==Overview==

We have determined the crystal structure of alpha-pokeweed antiviral, protein, a member of ribosome-inactivating proteins, at 0.23 nm, resolution, by the molecular-replacement method. The crystals belong to, the space group P2(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63, and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on, a crystal volume/unit protein molecular mass of 2.1 x 10(-3) nm3/Da. The, crystallographic residual value was reduced to 17.2% (0.6-0.23 nm, resolution) with root-mean-square deviations in bond lengths of 1.9 pm and, bond angles of 2.2 degrees. The C alpha-C alpha distance map shows that, alpha-pokeweed antiviral protein is composed of three modules, the, N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal, (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft, between the central and C-terminal modules and all the active residues, exist on the central module. The electrostatic potential around the, substrate-binding site shows that the central and C-terminal module sides, of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a, suitable interaction with the substrate rRNA.

We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63 and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on a crystal volume/unit protein molecular mass of 2.1 x 10(-3) nm3/Da. The crystallographic residual value was reduced to 17.2% (0.6-0.23 nm resolution) with root-mean-square deviations in bond lengths of 1.9 pm and bond angles of 2.2 degrees. The C alpha-C alpha distance map shows that alpha-pokeweed antiviral protein is composed of three modules, the N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft between the central and C-terminal modules and all the active residues exist on the central module. The electrostatic potential around the substrate-binding site shows that the central and C-terminal module sides of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a suitable interaction with the substrate rRNA.

==About this Structure==

1APA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1APA OCA].

1APA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APA OCA].

==Reference==

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[[Category: genomic clone]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 11:01:~~13 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1apa.gif|left|200px]]<br /><applet load="1apa" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1apa.gif|left|200px]]<br /><applet load="1apa" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1apa, resolution 2.3&Aring;" />
 '''X-RAY STRUCTURE OF A POKEWEED ANTIVIRAL PROTEIN, CODED BY A NEW GENOMIC CLONE, AT 0.23 NM RESOLUTION. A MODEL STRUCTURE PROVIDES A SUITABLE ELECTROSTATIC FIELD FOR SUBSTRATE BINDING.'''<br />
 ==Overview==
-We have determined the crystal structure of alpha-pokeweed antiviral, protein, a member of ribosome-inactivating proteins, at 0.23 nm, resolution, by the molecular-replacement method. The crystals belong to, the space group P2(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63, and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on, a crystal volume/unit protein molecular mass of 2.1 x 10(-3) nm3/Da. The, crystallographic residual value was reduced to 17.2% (0.6-0.23 nm, resolution) with root-mean-square deviations in bond lengths of 1.9 pm and, bond angles of 2.2 degrees. The C alpha-C alpha distance map shows that, alpha-pokeweed antiviral protein is composed of three modules, the, N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal, (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft, between the central and C-terminal modules and all the active residues, exist on the central module. The electrostatic potential around the, substrate-binding site shows that the central and C-terminal module sides, of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a, suitable interaction with the substrate rRNA.
+We have determined the crystal structure of alpha-pokeweed antiviral protein, a member of ribosome-inactivating proteins, at 0.23 nm resolution, by the molecular-replacement method. The crystals belong to the space group P2(1)2(1)2 with unit-cell dimensions a = 4.71, b = 11.63 and c = 4.96 nm, and contain one protein molecule/asymmetric unit based on a crystal volume/unit protein molecular mass of 2.1 x 10(-3) nm3/Da. The crystallographic residual value was reduced to 17.2% (0.6-0.23 nm resolution) with root-mean-square deviations in bond lengths of 1.9 pm and bond angles of 2.2 degrees. The C alpha-C alpha distance map shows that alpha-pokeweed antiviral protein is composed of three modules, the N-terminal (Ala1-Leu76), the central (Tyr77-Lys185) and the C-terminal (Tyr186-Thr266) modules. The substrate-binding site is formed as a cleft between the central and C-terminal modules and all the active residues exist on the central module. The electrostatic potential around the substrate-binding site shows that the central and C-terminal module sides of this cleft have a negatively and a positively charged region, respectively. This charge distribution in the protein seems to provide a suitable interaction with the substrate rRNA.
 ==About this Structure==
-APA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APA OCA].
+APA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytolacca_americana Phytolacca americana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APA OCA].
 ==Reference==
@@ Line 23: / Line 23: @@
 [[Category: genomic clone]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:01:13 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:55 2008''