1dbx: Difference between revisions

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

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

caption="1dbx, resolution 1.8Å" />

'''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)'''<br />

==Overview==

Structural genomics of proteins of unknown function most straightforwardly, assists with assignment of biochemical activity when the new structure, resembles that of proteins whose functions are known. When a new fold is, revealed, the universe of known folds is enriched, and once the function, is determined by other means, novel structure-function relationships are, established. The previously unannotated protein HI1434 from H. influenzae, provides a hybrid example of these two paradigms. It is a member of a, microbial protein family, labeled in SwissProt as YbaK and ebsC. The, crystal structure at 1.8 A resolution reported here reveals a fold that is, only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are, saccharide binding proteins. However, a crevice that may accommodate a, small ligand is evident. The putative binding site contains only one, invariant residue, Lys46, which carries a functional group that could play, a role in catalysis, indicating that YbaK is probably not an enzyme., Detailed sequence analysis, including a number of newly sequenced, microbial organisms, highlights sequence homology to an insertion domain, in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose, function is unknown. A HI1434-based model of the insertion domain shows, that it should also contain the putative binding site. Being part of a, tRNA synthetases, the insertion domain is likely to be involved in, oligonucleotide binding, with possible roles in recognition/discrimination, or editing of prolyl-tRNA. By analogy, YbaK may also play a role in, nucleotide or oligonucleotide binding, the nature of which is yet to be, determined.

Structural genomics of proteins of unknown function most straightforwardly assists with assignment of biochemical activity when the new structure resembles that of proteins whose functions are known. When a new fold is revealed, the universe of known folds is enriched, and once the function is determined by other means, novel structure-function relationships are established. The previously unannotated protein HI1434 from H. influenzae provides a hybrid example of these two paradigms. It is a member of a microbial protein family, labeled in SwissProt as YbaK and ebsC. The crystal structure at 1.8 A resolution reported here reveals a fold that is only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are saccharide binding proteins. However, a crevice that may accommodate a small ligand is evident. The putative binding site contains only one invariant residue, Lys46, which carries a functional group that could play a role in catalysis, indicating that YbaK is probably not an enzyme. Detailed sequence analysis, including a number of newly sequenced microbial organisms, highlights sequence homology to an insertion domain in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose function is unknown. A HI1434-based model of the insertion domain shows that it should also contain the putative binding site. Being part of a tRNA synthetases, the insertion domain is likely to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. By analogy, YbaK may also play a role in nucleotide or oligonucleotide binding, the nature of which is yet to be determined.

==About this Structure==

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

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

==Reference==

Line 16:

[[Category: Huang, K.]]

[[Category: Li, Z.]]

[[Category: S2F, Structure.2.Function.Project.]]

[[Category: S2F, Structure 2.Function Project.]]

[[Category: Zhang, H.]]

[[Category: s2f]]

Line 23:

[[Category: ybak]]

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@@ Line 1: / Line 1: @@
-[[Image:1dbx.jpg|left|200px]]<br /><applet load="1dbx" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1dbx.jpg|left|200px]]<br /><applet load="1dbx" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1dbx, resolution 1.8&Aring;" />
 '''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)'''<br />
 ==Overview==
-Structural genomics of proteins of unknown function most straightforwardly, assists with assignment of biochemical activity when the new structure, resembles that of proteins whose functions are known. When a new fold is, revealed, the universe of known folds is enriched, and once the function, is determined by other means, novel structure-function relationships are, established. The previously unannotated protein HI1434 from H. influenzae, provides a hybrid example of these two paradigms. It is a member of a, microbial protein family, labeled in SwissProt as YbaK and ebsC. The, crystal structure at 1.8 A resolution reported here reveals a fold that is, only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are, saccharide binding proteins. However, a crevice that may accommodate a, small ligand is evident. The putative binding site contains only one, invariant residue, Lys46, which carries a functional group that could play, a role in catalysis, indicating that YbaK is probably not an enzyme., Detailed sequence analysis, including a number of newly sequenced, microbial organisms, highlights sequence homology to an insertion domain, in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose, function is unknown. A HI1434-based model of the insertion domain shows, that it should also contain the putative binding site. Being part of a, tRNA synthetases, the insertion domain is likely to be involved in, oligonucleotide binding, with possible roles in recognition/discrimination, or editing of prolyl-tRNA. By analogy, YbaK may also play a role in, nucleotide or oligonucleotide binding, the nature of which is yet to be, determined.
+Structural genomics of proteins of unknown function most straightforwardly assists with assignment of biochemical activity when the new structure resembles that of proteins whose functions are known. When a new fold is revealed, the universe of known folds is enriched, and once the function is determined by other means, novel structure-function relationships are established. The previously unannotated protein HI1434 from H. influenzae provides a hybrid example of these two paradigms. It is a member of a microbial protein family, labeled in SwissProt as YbaK and ebsC. The crystal structure at 1.8 A resolution reported here reveals a fold that is only remotely related to the C-lectin fold, in particular to endostatin, and thus is not sufficiently similar to imply that YbaK proteins are saccharide binding proteins. However, a crevice that may accommodate a small ligand is evident. The putative binding site contains only one invariant residue, Lys46, which carries a functional group that could play a role in catalysis, indicating that YbaK is probably not an enzyme. Detailed sequence analysis, including a number of newly sequenced microbial organisms, highlights sequence homology to an insertion domain in prolyl-tRNA synthetases (proRS) from prokaryote, a domain whose function is unknown. A HI1434-based model of the insertion domain shows that it should also contain the putative binding site. Being part of a tRNA synthetases, the insertion domain is likely to be involved in oligonucleotide binding, with possible roles in recognition/discrimination or editing of prolyl-tRNA. By analogy, YbaK may also play a role in nucleotide or oligonucleotide binding, the nature of which is yet to be determined.
 ==About this Structure==
-DBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DBX OCA].
+DBX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBX OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Huang, K.]]
 [[Category: Li, Z.]]
-[[Category: S2F, Structure.2.Function.Project.]]
+[[Category: S2F, Structure 2.Function Project.]]
 [[Category: Zhang, H.]]
 [[Category: s2f]]
@@ Line 23: / Line 23: @@
 [[Category: ybak]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:09:06 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:02 2008''