2hb5: Difference between revisions

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[[Image:2hb5.gif|left|200px]]<br /><applet load="2hb5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:2hb5.gif|left|200px]]<br /><applet load="2hb5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="2hb5, resolution 1.59Å" />

'''Crystal Structure of the Moloney Murine Leukemia Virus RNase H Domain'''<br />

==Overview==

A crystallographic study of the Moloney murine leukemia virus (Mo-MLV), RNase H domain was performed to provide information about its structure, and mechanism of action. These efforts resulted in the crystallization of, a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The, 1.6-Angstroms resolution structure resembles the known structures of the, human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H., The structure revealed the coordination of a magnesium ion within the, catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a, high density of basic charges on one side of the enzyme. Using a model of, the Mo-MLV structure superimposed upon a structure of HIV-1 reverse, transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H, secondary structures and individual amino acids were examined for their, potential roles in binding substrate. Identified regions included Mo-MLV, RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD, and its following loop. Most of the identified substrate-binding residues, corresponded with residues directly binding nucleotides in an RNase H from, Bacillus halodurans as observed in a cocrystal structure with RNA/DNA., Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1, revealed that a loop of the HIV-1 connection domain resides within the, same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain, may serve to recognize and bind the RNA/DNA substrate major groove.

A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The 1.6-Angstroms resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a high density of basic charges on one side of the enzyme. Using a model of the Mo-MLV structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H secondary structures and individual amino acids were examined for their potential roles in binding substrate. Identified regions included Mo-MLV RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD and its following loop. Most of the identified substrate-binding residues corresponded with residues directly binding nucleotides in an RNase H from Bacillus halodurans as observed in a cocrystal structure with RNA/DNA. Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1 revealed that a loop of the HIV-1 connection domain resides within the same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain may serve to recognize and bind the RNA/DNA substrate major groove.

==About this Structure==

2HB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moloney_murine_leukemia_virus Moloney murine leukemia virus] with MG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2HB5 OCA].

2HB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moloney_murine_leukemia_virus Moloney murine leukemia virus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HB5 OCA].

==Reference==

Line 14:

[[Category: Single protein]]

[[Category: Bingman, C.]]

[[Category: Goff, S.P.]]

[[Category: Goff, S P.]]

[[Category: Gregorio, G.G.]]

[[Category: Gregorio, G G.]]

[[Category: Hendrickson, W.A.]]

[[Category: Hendrickson, W A.]]

[[Category: Lim, D.]]

[[Category: Martinez-Hackert, E.]]

Line 23:

[[Category: rnase h]]

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@@ Line 1: / Line 1: @@
-[[Image:2hb5.gif|left|200px]]<br /><applet load="2hb5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2hb5.gif|left|200px]]<br /><applet load="2hb5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2hb5, resolution 1.59&Aring;" />
 '''Crystal Structure of the Moloney Murine Leukemia Virus RNase H Domain'''<br />
 ==Overview==
-A crystallographic study of the Moloney murine leukemia virus (Mo-MLV), RNase H domain was performed to provide information about its structure, and mechanism of action. These efforts resulted in the crystallization of, a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The, 1.6-Angstroms resolution structure resembles the known structures of the, human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H., The structure revealed the coordination of a magnesium ion within the, catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a, high density of basic charges on one side of the enzyme. Using a model of, the Mo-MLV structure superimposed upon a structure of HIV-1 reverse, transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H, secondary structures and individual amino acids were examined for their, potential roles in binding substrate. Identified regions included Mo-MLV, RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD, and its following loop. Most of the identified substrate-binding residues, corresponded with residues directly binding nucleotides in an RNase H from, Bacillus halodurans as observed in a cocrystal structure with RNA/DNA., Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1, revealed that a loop of the HIV-1 connection domain resides within the, same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain, may serve to recognize and bind the RNA/DNA substrate major groove.
+A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The 1.6-Angstroms resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a high density of basic charges on one side of the enzyme. Using a model of the Mo-MLV structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H secondary structures and individual amino acids were examined for their potential roles in binding substrate. Identified regions included Mo-MLV RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD and its following loop. Most of the identified substrate-binding residues corresponded with residues directly binding nucleotides in an RNase H from Bacillus halodurans as observed in a cocrystal structure with RNA/DNA. Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1 revealed that a loop of the HIV-1 connection domain resides within the same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain may serve to recognize and bind the RNA/DNA substrate major groove.
 ==About this Structure==
-HB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moloney_murine_leukemia_virus Moloney murine leukemia virus] with MG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HB5 OCA].
+HB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Moloney_murine_leukemia_virus Moloney murine leukemia virus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HB5 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Bingman, C.]]
-[[Category: Goff, S.P.]]
+[[Category: Goff, S P.]]
-[[Category: Gregorio, G.G.]]
+[[Category: Gregorio, G G.]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson, W A.]]
 [[Category: Lim, D.]]
 [[Category: Martinez-Hackert, E.]]
@@ Line 23: / Line 23: @@
 [[Category: rnase h]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:39:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:03 2008''