1or6

From Proteopedia

(Difference between revisions)

Revision as of 15:44, 9 February 2016

Crystal Structure of HemAT sensor domain from B.subtilis in the unliganded form

Structural highlights

1or6 is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1or4
Gene:	yhfV ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[HEMAT_BACSU] Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.^[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

Much is now known about chemotaxis signaling transduction for Escherichia coli and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is, in a sense, reversed. Attractant binding strengthens the activity of histidine kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B. subtilis can detect oxygen and transmit the signal to regulatory proteins that control the direction of flagella rotation. We have determined the crystal structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A and 2.7 A resolution, respectively. The liganded structure reveals a highly symmetrical organization. Tyrosine70 shows distinct conformational changes on one subunit when ligands are removed. Our study suggests that disruption of the symmetry of HemAT plays an important role in initiating the chemotaxis signaling transduction cascade.

Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry.,Zhang W, Phillips GN Jr Structure. 2003 Sep;11(9):1097-110. PMID:12962628^[2]

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

References

↑ Hou S, Larsen RW, Boudko D, Riley CW, Karatan E, Zimmer M, Ordal GW, Alam M. Myoglobin-like aerotaxis transducers in Archaea and Bacteria. Nature. 2000 Feb 3;403(6769):540-4. PMID:10676961 doi:http://dx.doi.org/10.1038/35000570
↑ Zhang W, Phillips GN Jr. Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry. Structure. 2003 Sep;11(9):1097-110. PMID:12962628

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/1or6"

Categories: Bacillus globigii migula 1900 | Phillips, G N | Zhang, W | Globin fold | Signaling protein

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     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1or6 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1or6

From Proteopedia

Revision as of 15:44, 9 February 2016

Crystal Structure of HemAT sensor domain from B.subtilis in the unliganded form

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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