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PDBsum entry 1w3e

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Ribosomal protein PDB id
1w3e
Contents
Protein chain
99 a.a.
Waters ×87

References listed in PDB file
Key reference
Title Role of proline residues in thermostability of t. Celer l30e protein
Authors H.W.Ma, C.F.Lee, M.D.Allen, M.Bycroft, K.B.Wong.
Ref. To be Published ...
Secondary reference #1
Title Solution structure and thermal stability of ribosomal protein l30e from hyperthermophilic archaeon thermococcus celer.
Authors K.B.Wong, C.F.Lee, S.H.Chan, T.Y.Leung, Y.W.Chen, M.Bycroft.
Ref. Protein Sci, 2003, 12, 1483-1495. [DOI no: 10.1110/ps.0302303]
PubMed id 12824494
Full text Abstract
Figure 4.
Figure 4. Helix-4 of T. celer L30e is structured. (A) Ensembles of NMR structure of helix 4 of T. celer (black) and yeast (gray) L30e. Note that helix-4 is well defined in the structure of T. celer L30e but is more disordered in the yeast homolog. The arrow indicates the first turn of helix-4 of the yeast L30e, which is unstructured. (B) The amino -terminal of helix-4 of T. celer L30e is stabilized by capping. The hydroxyl group of Thr-66 forms a hydrogen bond to the backbone amide of Glu-69 at the amino- terminal of helix-4.
Figure 6.
Figure 6. Stereo-diagram showing hydrogen bond networks among buried polar groups of T30, S39, T65, and S91 in yeast L30e.
The above figures are reproduced from the cited reference with permission from the Protein Society
Secondary reference #2
Title Crystal structure of ribosomal protein l30e from the extreme thermophile thermococcus celer: thermal stability and RNA binding.
Authors Y.W.Chen, M.Bycroft, K.B.Wong.
Ref. Biochemistry, 2003, 42, 2857-2865. [DOI no: 10.1021/bi027131s]
PubMed id 12627951
Full text Abstract
PROCHECK
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