6a2j

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Crystal structure of heme A synthase from Bacillus subtilis

<StructureSection load='6a2j' size='340' side='right' caption='6a2j, resolution 2.20Å' scene=>

Structural highlights

6a2j is a 1 chain structure with sequence from Bacsu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:<scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
Gene:ctaA, BSU14870 (BACSU)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CTAA_BACSU] Catalyzes the oxidation of the C8 methyl side group on heme O porphyrin ring into a formyl group. Also involved in the sporulation.[1]

Publication Abstract from PubMed

Heme A is an essential cofactor for respiratory terminal oxidases and vital for respiration in aerobic organisms. The final step of heme A biosynthesis is formylation of the C-8 methyl group of heme molecule by heme A synthase (HAS). HAS is a heme-containing integral membrane protein, and its structure and reaction mechanisms have remained unknown. Thus, little is known about HAS despite of its importance. Here we report the crystal structure of HAS from Bacillus subtilis at 2.2-A resolution. The N- and C-terminal halves of HAS consist of four-helix bundles and they align in a pseudo twofold symmetry manner. Each bundle contains a pair of histidine residues and forms a heme-binding domain. The C-half domain binds a cofactor-heme molecule, while the N-half domain is vacant. Many water molecules are found in the transmembrane region and around the substrate-binding site, and some of them interact with the main chain of transmembrane helix. Comparison of these two domain structures enables us to construct a substrate-heme binding state structure. This structure implies that a completely conserved glutamate, Glu57 in B. subtilis, is the catalytic residue for the formylation reaction. These results provide valuable suggestions of the substrate-heme binding mechanism. Our results present significant insight into the heme A biosynthesis.

Crystal structure of heme A synthase from Bacillus subtilis.,Niwa S, Takeda K, Kosugi M, Tsutsumi E, Mogi T, Miki K Proc Natl Acad Sci U S A. 2018 Nov 20;115(47):11953-11957. doi:, 10.1073/pnas.1813346115. Epub 2018 Nov 5. PMID:30397130[2]

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

References

  1. ↑ Brown KR, Allan BM, Do P, Hegg EL. Identification of novel hemes generated by heme A synthase: evidence for two successive monooxygenase reactions. Biochemistry. 2002 Sep 10;41(36):10906-13. PMID:12206660
  2. ↑ Niwa S, Takeda K, Kosugi M, Tsutsumi E, Mogi T, Miki K. Crystal structure of heme A synthase from Bacillus subtilis. Proc Natl Acad Sci U S A. 2018 Nov 20;115(47):11953-11957. doi:, 10.1073/pnas.1813346115. Epub 2018 Nov 5. PMID:30397130 doi:http://dx.doi.org/10.1073/pnas.1813346115

Contents

</StructureSection>

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