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3bii

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{{STRUCTURE_3bii| PDB=3bii | SCENE= }}
{{STRUCTURE_3bii| PDB=3bii | SCENE= }}
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'''Crystal Structure of Activated MPT Synthase'''
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===Crystal Structure of Activated MPT Synthase===
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==Overview==
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In almost all biological life forms, molybdenum and tungsten are coordinated by molybdopterin (MPT), a tricyclic pyranopterin containing a cis-dithiolene group. Together, the metal and the pterin moiety form the redox reactive molybdenum cofactor (Moco). Mutations in patients with deficiencies in Moco biosynthesis usually occur in the enzymes catalyzing the first and second steps of biosynthesis, leading to the formation of precursor Z and MPT, respectively. The second step is catalyzed by the heterotetrameric MPT synthase protein consisting of two large (MoaE) and two small (MoaD) subunits with the MoaD subunits located at opposite ends of a central MoaE dimer. Previous studies have determined that the conversion of the sulfur- and metal-free precursor Z to MPT by MPT synthase involves the transfer of sulfur atoms from a C-terminal MoaD thiocarboxylate to the C-1' and C-2' positions of precursor Z. Here, we present the crystal structures of non-thiocarboxylated MPT synthase from Staphylococcus aureus in its apo form and in complex with precursor Z. A comparison of the two structures reveals conformational changes in a loop that participates in interactions with precursor Z. In the complex, precursor Z is bound by strictly conserved residues in a pocket at the MoaE dimer interface in close proximity of the C-terminal glycine of MoaD. Biochemical evidence indicates that the first dithiolene sulfur is added at the C-2' position.
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(as it appears on PubMed at http://www.pubmed.gov), where 18092812 is the PubMed ID number.
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{{ABSTRACT_PUBMED_18092812}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency., Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H, Biochemistry. 2008 Jan 15;47(2):615-26. Epub 2007 Dec 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18092812 18092812]
Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency., Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H, Biochemistry. 2008 Jan 15;47(2):615-26. Epub 2007 Dec 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18092812 18092812]
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Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12571227 12571227]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Ubiquitin-like]]
[[Category: Ubiquitin-like]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:48:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:24:49 2008''

Revision as of 17:24, 27 July 2008

Image:3bii.png

Template:STRUCTURE 3bii

Crystal Structure of Activated MPT Synthase

Template:ABSTRACT PUBMED 18092812

About this Structure

3BII is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of a molybdopterin synthase-precursor Z complex: insight into its sulfur transfer mechanism and its role in molybdenum cofactor deficiency., Daniels JN, Wuebbens MM, Rajagopalan KV, Schindelin H, Biochemistry. 2008 Jan 15;47(2):615-26. Epub 2007 Dec 20. PMID:18092812

Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:12571227

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