9rnt: Difference between revisions

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[[Image:9rnt.jpg|left|200px]]<br /><applet load="9rnt" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:9rnt.jpg|left|200px]]<br /><applet load="9rnt" size="350" color="white" frame="true" align="right" spinBox="true"

caption="9rnt, resolution 1.5Å" />

'''RIBONUCLEASE T1 WITH FREE RECOGNITION AND CATALYTIC SITE: CRYSTAL STRUCTURE ANALYSIS AT 1.5 ANGSTROMS RESOLUTION'''<br />

==Overview==

The free form of ribonuclease T1 (RNase T1) has been crystallized at, neutral pH, and the three-dimensional structure of the enzyme has been, determined at 1.5 A nominal resolution. Restrained least-squares, refinement yielded an R value of 14.3% for 12,623 structure amplitudes., The high resolution of the structure analysis permits a detailed, description of the solvent structure around RNase T1, the reliable, rotational setting of several side-chain amide and imidazole groups and, the identification of seven disordered residues. Among these, the, disordered and completely internal Val78 residue is noteworthy. In the, RNase T1 crystal structures determined thus far it is always disordered in, the absence of bound guanosine, but not in its presence. A systematic, analysis of hydrogen bonding reveals the presence in RNase T1 of 40, three-center and an additional seven four-center hydrogen bonds., Three-center hydrogen bonds occur predominantly in the alpha-helix, where, their minor components close 3(10)-type turns, and in beta-sheets, where, their minor components connect the peptide nitrogen and carbonyl functions, of the same residue. The structure of the free form is compared with, complexes of RNase T1 with filled base recognition site and/or catalytic, site. Several structural rearrangements occurring upon inhibitor or, substrate binding are clearly apparent. In conjunction with the available, biochemical knowledge, they are used to describe probable steps occurring, early during RNase T1-catalyzed phosphate transesterification.

The free form of ribonuclease T1 (RNase T1) has been crystallized at neutral pH, and the three-dimensional structure of the enzyme has been determined at 1.5 A nominal resolution. Restrained least-squares refinement yielded an R value of 14.3% for 12,623 structure amplitudes. The high resolution of the structure analysis permits a detailed description of the solvent structure around RNase T1, the reliable rotational setting of several side-chain amide and imidazole groups and the identification of seven disordered residues. Among these, the disordered and completely internal Val78 residue is noteworthy. In the RNase T1 crystal structures determined thus far it is always disordered in the absence of bound guanosine, but not in its presence. A systematic analysis of hydrogen bonding reveals the presence in RNase T1 of 40 three-center and an additional seven four-center hydrogen bonds. Three-center hydrogen bonds occur predominantly in the alpha-helix, where their minor components close 3(10)-type turns, and in beta-sheets, where their minor components connect the peptide nitrogen and carbonyl functions of the same residue. The structure of the free form is compared with complexes of RNase T1 with filled base recognition site and/or catalytic site. Several structural rearrangements occurring upon inhibitor or substrate binding are clearly apparent. In conjunction with the available biochemical knowledge, they are used to describe probable steps occurring early during RNase T1-catalyzed phosphate transesterification.

==About this Structure==

9RNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=9RNT OCA].

9RNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RNT OCA].

==Reference==

Line 20:

[[Category: hydrolase(endoribonuclease)]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 12~~:58:~~09 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:9rnt.jpg|left|200px]]<br /><applet load="9rnt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:9rnt.jpg|left|200px]]<br /><applet load="9rnt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="9rnt, resolution 1.5&Aring;" />
 '''RIBONUCLEASE T1 WITH FREE RECOGNITION AND CATALYTIC SITE: CRYSTAL STRUCTURE ANALYSIS AT 1.5 ANGSTROMS RESOLUTION'''<br />
 ==Overview==
-The free form of ribonuclease T1 (RNase T1) has been crystallized at, neutral pH, and the three-dimensional structure of the enzyme has been, determined at 1.5 A nominal resolution. Restrained least-squares, refinement yielded an R value of 14.3% for 12,623 structure amplitudes., The high resolution of the structure analysis permits a detailed, description of the solvent structure around RNase T1, the reliable, rotational setting of several side-chain amide and imidazole groups and, the identification of seven disordered residues. Among these, the, disordered and completely internal Val78 residue is noteworthy. In the, RNase T1 crystal structures determined thus far it is always disordered in, the absence of bound guanosine, but not in its presence. A systematic, analysis of hydrogen bonding reveals the presence in RNase T1 of 40, three-center and an additional seven four-center hydrogen bonds., Three-center hydrogen bonds occur predominantly in the alpha-helix, where, their minor components close 3(10)-type turns, and in beta-sheets, where, their minor components connect the peptide nitrogen and carbonyl functions, of the same residue. The structure of the free form is compared with, complexes of RNase T1 with filled base recognition site and/or catalytic, site. Several structural rearrangements occurring upon inhibitor or, substrate binding are clearly apparent. In conjunction with the available, biochemical knowledge, they are used to describe probable steps occurring, early during RNase T1-catalyzed phosphate transesterification.
+The free form of ribonuclease T1 (RNase T1) has been crystallized at neutral pH, and the three-dimensional structure of the enzyme has been determined at 1.5 A nominal resolution. Restrained least-squares refinement yielded an R value of 14.3% for 12,623 structure amplitudes. The high resolution of the structure analysis permits a detailed description of the solvent structure around RNase T1, the reliable rotational setting of several side-chain amide and imidazole groups and the identification of seven disordered residues. Among these, the disordered and completely internal Val78 residue is noteworthy. In the RNase T1 crystal structures determined thus far it is always disordered in the absence of bound guanosine, but not in its presence. A systematic analysis of hydrogen bonding reveals the presence in RNase T1 of 40 three-center and an additional seven four-center hydrogen bonds. Three-center hydrogen bonds occur predominantly in the alpha-helix, where their minor components close 3(10)-type turns, and in beta-sheets, where their minor components connect the peptide nitrogen and carbonyl functions of the same residue. The structure of the free form is compared with complexes of RNase T1 with filled base recognition site and/or catalytic site. Several structural rearrangements occurring upon inhibitor or substrate binding are clearly apparent. In conjunction with the available biochemical knowledge, they are used to describe probable steps occurring early during RNase T1-catalyzed phosphate transesterification.
 ==About this Structure==
-RNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=9RNT OCA].
+RNT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RNT OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: hydrolase(endoribonuclease)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:58:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:18:55 2008''