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Article: Crystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis

TitleCrystal structure of uroporphyrinogen decarboxylase from Bacillus subtilis
Authors
Issue Date2007
PublisherAmerican Society for Microbiology
Citation
Journal Of Bacteriology, 2007, v. 189 n. 9, p. 3573-3580 How to Cite?
AbstractUroporphyrinogen decarboxylase (UROD) is a branch point enzyme in the biosynthesis of the tetrapyrroles. It catalyzes the decarboxylation of four acetate groups of uroporphyrinogen III to yield coproporphyrinogen III, leading to heme and chlorophyll biosynthesis. UROD is a special type of nonoxidative decarboxylase, since no cofactor is essential for catalysis. In this work, the first crystal structure of a bacterial UROD, Bacillus subtilis UROD (UROD Bs), has been determined at a 2.3 Å resolution. The biological unit of UROD Bs was determined by dynamic light scattering measurements to be a homodimer in solution. There are four molecules in the crystallographic asymmetric unit, corresponding to two homodimers. Structural comparison of UROD Bs with eukaryotic URODs reveals a variation of two loops, which possibly affect the binding of substrates and release of products. Structural comparison with the human UROD-coproporphyrinogen III complex discloses a similar active cleft, with five invariant polar residues (Arg29, Arg33, Asp78, Tyr154, and His322) and three invariant hydrophobic residues (Ile79, Phe144, and Phe207), in UROD Bs. Among them, Asp78 may interact with the pyrrole NH groups of the substrate, and Arg29 is a candidate for positioning the acetate groups of the substrate. Both residues may also play catalytic roles. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91937
ISSN
2015 Impact Factor: 3.198
2015 SCImago Journal Rankings: 2.216
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFan, Jen_HK
dc.contributor.authorLiu, Qen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorTeng, Men_HK
dc.contributor.authorNiu, Len_HK
dc.date.accessioned2010-09-17T10:31:04Z-
dc.date.available2010-09-17T10:31:04Z-
dc.date.issued2007en_HK
dc.identifier.citationJournal Of Bacteriology, 2007, v. 189 n. 9, p. 3573-3580en_HK
dc.identifier.issn0021-9193en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91937-
dc.description.abstractUroporphyrinogen decarboxylase (UROD) is a branch point enzyme in the biosynthesis of the tetrapyrroles. It catalyzes the decarboxylation of four acetate groups of uroporphyrinogen III to yield coproporphyrinogen III, leading to heme and chlorophyll biosynthesis. UROD is a special type of nonoxidative decarboxylase, since no cofactor is essential for catalysis. In this work, the first crystal structure of a bacterial UROD, Bacillus subtilis UROD (UROD Bs), has been determined at a 2.3 Å resolution. The biological unit of UROD Bs was determined by dynamic light scattering measurements to be a homodimer in solution. There are four molecules in the crystallographic asymmetric unit, corresponding to two homodimers. Structural comparison of UROD Bs with eukaryotic URODs reveals a variation of two loops, which possibly affect the binding of substrates and release of products. Structural comparison with the human UROD-coproporphyrinogen III complex discloses a similar active cleft, with five invariant polar residues (Arg29, Arg33, Asp78, Tyr154, and His322) and three invariant hydrophobic residues (Ile79, Phe144, and Phe207), in UROD Bs. Among them, Asp78 may interact with the pyrrole NH groups of the substrate, and Arg29 is a candidate for positioning the acetate groups of the substrate. Both residues may also play catalytic roles. Copyright © 2007, American Society for Microbiology. All Rights Reserved.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiologyen_HK
dc.relation.ispartofJournal of Bacteriologyen_HK
dc.titleCrystal structure of uroporphyrinogen decarboxylase from Bacillus subtilisen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1128/JB.01083-06en_HK
dc.identifier.pmid17122346-
dc.identifier.pmcidPMC1855892-
dc.identifier.scopuseid_2-s2.0-34247601638en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-34247601638&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume189en_HK
dc.identifier.issue9en_HK
dc.identifier.spage3573en_HK
dc.identifier.epage3580en_HK
dc.identifier.isiWOS:000246028400026-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridFan, J=36672761400en_HK
dc.identifier.scopusauthoridLiu, Q=35215401600en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridTeng, M=7101891754en_HK
dc.identifier.scopusauthoridNiu, L=7101760477en_HK

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