Novel re-arrangement of an RsmA/cSRa family protein to create a structurally distinct new RNA-binding family member

> Summary

Summary for 4KJI

DescriptorRsmN, a RNA-binding protein of Regulator of Secondary Metabolism, RsmZ-2 (2 entities in total)
Functional Keywordsprotein-rna complex, beta barrel, beta-barrel, post-transcriptional regulation, rna binding, rna binding protein-rna complex, rna binding protein/rna
Biological sourcePseudomonas aeruginosa
Total number of polymer chains4
Total molecular weight27918.8
Li, C. (deposition date: 2013-05-03, release date: 2013-09-04, Last modification date: 2013-09-25)
Primary citation
Morris, E.R.,Hall, G.,Li, C.,Heeb, S.,Kulkarni, R.V.,Lovelock, L.,Silistre, H.,Messina, M.,Camara, M.,Emsley, J.,Williams, P.,Searle, M.S.
Structural Rearrangement in an RsmA/CsrA Ortholog of Pseudomonas aeruginosa Creates a Dimeric RNA-Binding Protein, RsmN.
Structure, 21:1659-1671, 2013
PubMed: 23954502 (PDB entries with the same primary citation)
DOI: 10.1016/j.str.2013.07.007
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliersRNA backbone0.323622.4%30.2%0.6%0.26MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 4kji
no rotation
Molmil generated image of 4kji
rotated about x axis by 90°
Molmil generated image of 4kji
rotated about y axis by 90°

> Structural details


Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
A, BRsmN, a RNA-binding protein of Regulator of Secondary Metabolismpolymer798768.22
UniProt (Q02EI1)
Pfam (PF02599)
UniProt (by SIFTS) (A0A0H2ZIZ8)
Pseudomonas aeruginosa
C, DRsmZ-2polymer165191.22

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains4
Total molecular weight27918.8
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight27918.8
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (3.2 Å)

Cell axes83.64983.64994.239
Cell angles90.0090.0090.00
SpacegroupP 43 2 2
Resolution limits29.56 - 3.20
the highest resolution shell value3.280 - 3.200
the highest resolution shell value0.372
the highest resolution shell value0.462
RMSD bond length0.013
RMSD bond angle1.718

Data Collection Statistics

Resolution limits29.57 - 3.20
the highest resolution shell value -
Number of reflections5917
the highest resolution shell value6.1

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*

> Functional details


Functional Information from GO Data

A0003723molecular_functionRNA binding
A0006402biological_processmRNA catabolic process
A0006109biological_processregulation of carbohydrate metabolic process
B0003723molecular_functionRNA binding
B0006402biological_processmRNA catabolic process
B0006109biological_processregulation of carbohydrate metabolic process

Functional Information from PDB Data

site_idNumber of ResiduesDetails

Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails

Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails

Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails

Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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