1j93

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[[Image:1j93.jpg|left|200px]]<br /><applet load="1j93" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j93.jpg|left|200px]]
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caption="1j93, resolution 2.30&Aring;" />
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'''Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism'''<br />
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{{Structure
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|PDB= 1j93 |SIZE=350|CAPTION= <scene name='initialview01'>1j93</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Uroporphyrinogen_decarboxylase Uroporphyrinogen decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.37 4.1.1.37]
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|GENE=
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}}
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'''Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1J93 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Uroporphyrinogen_decarboxylase Uroporphyrinogen decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.37 4.1.1.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J93 OCA].
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1J93 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J93 OCA].
==Reference==
==Reference==
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Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism., Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A, J Biol Chem. 2001 Nov 23;276(47):44108-16. Epub 2001 Aug 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11524417 11524417]
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Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism., Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A, J Biol Chem. 2001 Nov 23;276(47):44108-16. Epub 2001 Aug 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11524417 11524417]
[[Category: Nicotiana tabacum]]
[[Category: Nicotiana tabacum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: plastidial enzyme]]
[[Category: plastidial enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:00:14 2008''

Revision as of 10:00, 20 March 2008


PDB ID 1j93

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Activity: Uroporphyrinogen decarboxylase, with EC number 4.1.1.37
Coordinates: save as pdb, mmCIF, xml



Crystal Structure and Substrate Binding Modeling of the Uroporphyrinogen-III Decarboxylase from Nicotiana tabacum: Implications for the Catalytic Mechanism


Overview

The enzymatic catalysis of many biological processes of life is supported by the presence of cofactors and prosthetic groups originating from the common tetrapyrrole precursor uroporphyrinogen-III. Uroporphyrinogen-III decarboxylase catalyzes its conversion into coproporphyrinogen-III, leading in plants to chlorophyll and heme biosynthesis. Here we report the first crystal structure of a plant (Nicotiana tabacum) uroporphyrinogen-III decarboxylase, together with the molecular modeling of substrate binding in tobacco and human enzymes. Its structural comparison with the homologous human protein reveals a similar catalytic cleft with six invariant polar residues, Arg(32), Arg(36), Asp(82), Ser(214) (Thr in Escherichia coli), Tyr(159), and His(329) (tobacco numbering). The functional relationships obtained from the structural and modeling analyses of both enzymes allowed the proposal for a refined catalytic mechanism. Asp(82) and Tyr(159) seem to be the catalytic functional groups, whereas the other residues may serve in substrate recognition and binding, with Arg(32) steering its insertion. The crystallographic dimer appears to represent the protein dimer under physiological conditions. The dimeric arrangement offers a plausible mechanism at least for the first two (out of four) decarboxylation steps.

About this Structure

1J93 is a Single protein structure of sequence from Nicotiana tabacum. Full crystallographic information is available from OCA.

Reference

Crystal structure and substrate binding modeling of the uroporphyrinogen-III decarboxylase from Nicotiana tabacum. Implications for the catalytic mechanism., Martins BM, Grimm B, Mock HP, Huber R, Messerschmidt A, J Biol Chem. 2001 Nov 23;276(47):44108-16. Epub 2001 Aug 27. PMID:11524417

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