1dbx
From Proteopedia
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| - | [[Image:1dbx.jpg|left|200px]] | + | [[Image:1dbx.jpg|left|200px]] |
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| - | '''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)''' | + | {{Structure |
| + | |PDB= 1dbx |SIZE=350|CAPTION= <scene name='initialview01'>1dbx</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= YbaK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of cysteinyl-tRNA(Pro) deacylase from H. influenzae (HI1434)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DBX is a [ | + | 1DBX is a [[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== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10813833 10813833] |
[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Zhang, H.]] | [[Category: Zhang, H.]] | ||
[[Category: s2f]] | [[Category: s2f]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[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 Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:59 2008'' |
Revision as of 08:36, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | YbaK (Haemophilus influenzae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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
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