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| | '''Urease accessory protein''' (Ure) is a Ni-containing urea hydrolase involved in nitrogen recycling from arginine, ureide and purines. Ure proteins are involved in urease activation by the transfer of Ni into the protein<ref>PMID:11289508</ref>. | | '''Urease accessory protein''' (Ure) is a Ni-containing urea hydrolase involved in nitrogen recycling from arginine, ureide and purines. Ure proteins are involved in urease activation by the transfer of Ni into the protein<ref>PMID:11289508</ref>. |
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| | + | *'''UreD''' - required for nickel incorporation <ref>PMID:12471450</ref>.<br /> |
| | *'''UreE''' - see [[Molecular Playground/UreE]].<br /> | | *'''UreE''' - see [[Molecular Playground/UreE]].<br /> |
| | *'''UreF''' - modulates the activation process of urease by eliminating the binding of Ni irons to noncarbamylated protein<ref>PMID:8808930</ref>.<br /> | | *'''UreF''' - modulates the activation process of urease by eliminating the binding of Ni irons to noncarbamylated protein<ref>PMID:8808930</ref>.<br /> |
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| | == Structural highlights == | | == Structural highlights == |
| | The <scene name='59/590652/Cv/3'>Ni+2 ion coordinates ligands which include 3 His residues belonging to the two monomers, water molecule</scene><ref>PMID:22010876</ref>. Water molecule is shown as red sphere. | | The <scene name='59/590652/Cv/3'>Ni+2 ion coordinates ligands which include 3 His residues belonging to the two monomers, water molecule</scene><ref>PMID:22010876</ref>. Water molecule is shown as red sphere. |
| - | </StructureSection> | |
| | | | |
| | ==3D structures of urease accessory protein== | | ==3D structures of urease accessory protein== |
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
| + | [[Urease accessory protein 3D structures]] |
| - | {{#tree:id=OrganizedByTopic|openlevels=0|
| + | |
| - | | + | |
| - | *Urease accessory protein E
| + | |
| - | | + | |
| - | **[[1gmv]], [[1gmu]] – KaUreE residues 1-143 (mutant) – ''Klebsiella aerogenes''<br />
| + | |
| - | **[[1gmw]] – KaUreE residues 1-143 (mutant) + Cu <br />
| + | |
| - | **[[4l3k]] – UreE + Zn + Ni – ''Sporosarcina pasteurii''<br />
| + | |
| - | **[[3tj8]], [[3ny0]] – HpUreE + Ni – ''Helicobacter pylori''<br />
| + | |
| - | **[[3tj9]] – HpUreE + Zn<br />
| + | |
| - | **[[3nxz]] – HpUreE + Cu<br />
| + | |
| - | **[[3la0]] – HpUreE + metal<br />
| + | |
| - | **[[3tja]], [[3l9z]] – HpUreE <br />
| + | |
| - | **[[1ear]], [[1eb0]] – UreE (mutant) + Zn – ''Bacillus pasteurii''<br />
| + | |
| - | **[[6jc4]] – KpUreE – ''Klebsiella pnemoniae''<br />
| + | |
| - | | + | |
| - | *Urease accessory protein F
| + | |
| - | | + | |
| - | **[[2wgl]], [[3cxn]], [[3o1q]] – HpUreF <br />
| + | |
| - | **[[3sf5]] – HpUreF + HpUreH<br />
| + | |
| - | **[[4hi0]] – HpUreF + HpUreG + HpUreH + GDP<br />
| + | |
| - | | + | |
| - | *Urease accessory protein G
| + | |
| - | | + | |
| - | **[[5xkt]] – KpUreG + GMPPNP + Ni <br />
| + | |
| - | | + | |
| - | *Urease accessory protein I
| + | |
| - | | + | |
| - | **[[3ux4]] – HpUreI <br />
| + | |
| - | }}
| + | |
| | | | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | + | </StructureSection> |
| | [[Category: Topic Page]] | | [[Category: Topic Page]] |
|
Function
Urease accessory protein (Ure) is a Ni-containing urea hydrolase involved in nitrogen recycling from arginine, ureide and purines. Ure proteins are involved in urease activation by the transfer of Ni into the protein[1].
- UreD - required for nickel incorporation [2].
- UreE - see Molecular Playground/UreE.
- UreF - modulates the activation process of urease by eliminating the binding of Ni irons to noncarbamylated protein[3].
- UreG - modulates the activation process of urease in plants [4].
- UreH - forms in combination with UreF and UreG a pre-activation complex which activates urease[5].
- UreI - probably facilitates nickel incorporation.
Structural highlights
The [6]. Water molecule is shown as red sphere.
3D structures of urease accessory protein
Urease accessory protein 3D structures
References
- ↑ Witte CP, Isidore E, Tiller SA, Davies HV, Taylor MA. Functional characterisation of urease accessory protein G (ureG) from potato. Plant Mol Biol. 2001 Jan;45(2):169-79. PMID:11289508
- ↑ Bacanamwo M, Witte CP, Lubbers MW, Polacco JC. Activation of the urease of Schizosaccharomyces pombe by the UreF accessory protein from soybean. Mol Genet Genomics. 2002 Dec;268(4):525-34. PMID:12471450 doi:10.1007/s00438-002-0769-z
- ↑ Moncrief MB, Hausinger RP. Purification and activation properties of UreD-UreF-urease apoprotein complexes. J Bacteriol. 1996 Sep;178(18):5417-21. PMID:8808930
- ↑ Myrach T, Zhu A, Witte CP. The assembly of the plant urease activation complex and the essential role of the urease accessory protein G (UreG) in delivery of nickel to urease. J Biol Chem. 2017 Sep 1;292(35):14556-14565. doi: 10.1074/jbc.M117.780403. Epub, 2017 Jul 14. PMID:28710280 doi:http://dx.doi.org/10.1074/jbc.M117.780403
- ↑ Fong YH, Wong HC, Chuck CP, Chen YW, Sun H, Wong KB. Assembly of Preactivation Complex for Urease Maturation in Helicobacter pylori: CRYSTAL STRUCTURE OF UreF-UreH PROTEIN COMPLEX. J Biol Chem. 2011 Dec 16;286(50):43241-9. Epub 2011 Oct 19. PMID:22013070 doi:10.1074/jbc.M111.296830
- ↑ Banaszak K, Martin-Diaconescu V, Bellucci M, Zambelli B, Rypniewski W, Maroney MJ, Ciurli S. Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveal a role for the disordered C-terminal arm in metal trafficking. Biochem J. 2011 Oct 20. PMID:22010876 doi:10.1042/BJ20111659
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