Structure of an essential bacterial protein YeaZ (TM0874) from Thermotoga maritima at 2.5 Å resolution

Xu, Q.; McMullan, D.; Jaroszewski, L.; Krishna, S.S.; Elsliger, M.-A.; Yeh, A.P.; Abdubek, P.; Astakhova, T.; Axelrod, H.L.; Carlton, D.; Chiu, H.-J.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grant, J.C.; Han, G.W.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Hodgson, K.O.; Wooley, J.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.

doi:10.1107/S1744309109022192

Acta Crystallographica Section F
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Figure 3
Mapping of conserved regions onto the TmYeaZ structure. (a) Ribbon representation of TmYeaZ colored by sequence conservation of 237 homologs of TmYeaZ. The most conserved residues are shown in magenta and the least conserved residues in cyan. The most conserved regions of the structure are marked 1, 2 and 3, respectively. (b) Molecular surface of TmYeaZ colored by sequence conservation. The orientation of the molecule is the same as in Fig. 2

(a). (c) A sequence logo representation of the three most conserved regions in YeaZ. A logo consists of stacks of symbols, one stack for each position in the sequence. The overall height of the stack indicates the sequence conservation at that position, while the height of the symbols within the stack indicates the relative frequency of each amino or nucleic acid at that position. (d, e) Molecular surface of the AB (d) and A₂ (or B₂) (e) dimers colored by sequence conservation, as in Figs. 1(b) and 1(c).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 10| October 2010| Pages 1230-1236

doi:10.1107/S1744309109022192

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