This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dbx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dbx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1dbx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dbx| PDB=1dbx | SCENE= }}
{{STRUCTURE_1dbx| PDB=1dbx | SCENE= }}
-
'''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)'''
+
===Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10813833}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10813833 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10813833}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Structure 2 function project]]
[[Category: Structure 2 function project]]
[[Category: Ybak]]
[[Category: Ybak]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:40:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:47:48 2008''

Revision as of 19:47, 30 June 2008

Image:1dbx.png

Template:STRUCTURE 1dbx

Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)

Template:ABSTRACT PUBMED 10813833

About this Structure

1DBX is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications., Zhang H, Huang K, Li Z, Banerjei L, Fisher KE, Grishin NV, Eisenstein E, Herzberg O, Proteins. 2000 Jul 1;40(1):86-97. PMID:10813833

Page seeded by OCA on Mon Jun 30 22:47:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dbx"
Personal tools