From Proteopedia
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| - | [[Image:1dbx.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1dbx| PDB=1dbx | SCENE= }} | | {{STRUCTURE_1dbx| PDB=1dbx | SCENE= }} |
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| - | '''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)'''
| + | ===Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_10813833}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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
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
