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.

1dcj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION

Structural highlights

1dcj is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TUSA_ECOLI Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Interacts with IscS and stimulates its activity. Then, accepts a sulfur from IscS and transfers it in turn to TusD. Seems to affect the stability of sigma-S, particularly during the logarithmic growth phase.^[1]

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

YhhP, a small protein of 81 amino acid residues encoded by the yhhP gene in the Escherichia coli database, is implicated in cell division although the precise biological function of this protein has not been yet identified. A variety of microorganisms have similar proteins, all of which contain a common CPxP sequence motif in the N-terminal region. We have determined the three-dimensional solution structure of YhhP by NMR spectroscopy in order to obtain insight into its biological function. It folds into a two-layered alpha/beta-sandwich structure with a betaalphabetaalphabetabeta fold, comprising a mixed four-stranded beta-sheet stacked against two alpha-helices, both of which are nearly parallel to the strands of the beta-sheet. The CPxP motif plays a significant structural role in stabilizing the first helix as a part of the new type N-capping box where the Cys-Pro peptide bond adopts a cis configuration. The structure of YhhP displays a striking resemblance to the C-terminal ribosome-binding domain of translation initiation factor IF3 (IF3C). In addition, the surface charge distribution of the RNA-recognition helix of IF3C is nearly the same as that of the corresponding helix of YhhP. These results suggest a structure-based hypothesis in which binding to an RNA target plays an essential role in the function of this ubiquitous protein.

High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division.,Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T J Mol Biol. 2000 Nov 24;304(2):219-29. PMID:11080457^[2]

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

References

↑ Ikeuchi Y, Shigi N, Kato J, Nishimura A, Suzuki T. Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell. 2006 Jan 6;21(1):97-108. PMID:16387657 doi:http://dx.doi.org/S1097-2765(05)01761-2
↑ Katoh E, Hatta T, Shindo H, Ishii Y, Yamada H, Mizuno T, Yamazaki T. High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. J Mol Biol. 2000 Nov 24;304(2):219-29. PMID:11080457 doi:http://dx.doi.org/10.1006/jmbi.2000.4170

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/1dcj"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION==
-<StructureSection load='1dcj' size='340' side='right'caption='[[1dcj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1dcj' size='340' side='right'caption='[[1dcj]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dcj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dcj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCJ FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcj OCA], [https://pdbe.org/1dcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcj RCSB], [https://www.ebi.ac.uk/pdbsum/1dcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcj ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcj OCA], [https://pdbe.org/1dcj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcj RCSB], [https://www.ebi.ac.uk/pdbsum/1dcj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/TUSA_ECOLI TUSA_ECOLI]] Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Interacts with IscS and stimulates its activity. Then, accepts a sulfur from IscS and transfers it in turn to TusD. Seems to affect the stability of sigma-S, particularly during the logarithmic growth phase.<ref>PMID:16387657</ref>
+[https://www.uniprot.org/uniprot/TUSA_ECOLI TUSA_ECOLI] Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Interacts with IscS and stimulates its activity. Then, accepts a sulfur from IscS and transfers it in turn to TusD. Seems to affect the stability of sigma-S, particularly during the logarithmic growth phase.<ref>PMID:16387657</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Hatta, T]]
+[[Category: Hatta T]]
-[[Category: Katoh, E]]
+[[Category: Katoh E]]
-[[Category: Mizuno, T]]
+[[Category: Mizuno T]]
-[[Category: Shindo, H]]
+[[Category: Shindo H]]
-[[Category: Yamazaki, T]]
+[[Category: Yamazaki T]]
-[[Category: Alpha-beta sandwich]]
-[[Category: Structural genomic]]
-[[Category: Unknown function]]

1dcj

From Proteopedia

Current revision

SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox