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1fbn

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Revision as of 09:59, 25 December 2014

CRYSTAL STRUCTURE OF A FIBRILLARIN HOMOLOGUE FROM METHANOCOCCUS JANNASCHII, A HYPERTHERMOPHILE, AT 1.6 A

Structural highlights

1fbn is a 1 chain structure with sequence from Atcc 43067. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, RCSB, PDBsum, TOPSAN

Function

[FLPA_METJA] Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity).[HAMAP-Rule:MF_00351]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Fibrillarin is a phylogenetically conserved protein essential for efficient processing of pre-rRNA through its association with a class of small nucleolar RNAs during ribosomal biogenesis. The protein is the antigen for the autoimmune disease scleroderma. Here we report the crystal structure of the fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. The structure consists of two domains, with a novel fold in the N-terminal region and a methyltransferase-like domain in the C-terminal region. Mapping temperature-sensitive mutations found in yeast fibrillarin Nop1 to the Methanococcus homologue structure reveals that many of the mutations cluster in the core of the methyltransferase-like domain.

Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution.,Wang H, Boisvert D, Kim KK, Kim R, Kim SH EMBO J. 2000 Feb 1;19(3):317-23. PMID:10654930^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang H, Boisvert D, Kim KK, Kim R, Kim SH. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. EMBO J. 2000 Feb 1;19(3):317-23. PMID:10654930 doi:10.1093/emboj/19.3.317

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fbn"

@@ Line 6: / Line 6: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fbn RCSB], [http://www.ebi.ac.uk/pdbsum/1fbn PDBsum], [http://www.topsan.org/Proteins/BSGC/1fbn TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FLPA_METJA FLPA_METJA]] Involved in pre-rRNA and tRNA processing. Utilizes the methyl donor S-adenosyl-L-methionine to catalyze the site-specific 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA (By similarity).[HAMAP-Rule:MF_00351]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fbn

From Proteopedia

Revision as of 09:59, 25 December 2014

CRYSTAL STRUCTURE OF A FIBRILLARIN HOMOLOGUE FROM METHANOCOCCUS JANNASCHII, A HYPERTHERMOPHILE, AT 1.6 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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