1n7h

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[[Image:1n7h.jpg|left|200px]]<br /><applet load="1n7h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n7h.jpg|left|200px]]
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caption="1n7h, resolution 1.8&Aring;" />
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'''Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP'''<br />
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{{Structure
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|PDB= 1n7h |SIZE=350|CAPTION= <scene name='initialview01'>1n7h</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/GDP-mannose_4,6-dehydratase GDP-mannose 4,6-dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.47 4.2.1.47]
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|GENE= mur1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])
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}}
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'''Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1N7H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=NDP:'>NDP</scene> and <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/GDP-mannose_4,6-dehydratase GDP-mannose 4,6-dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.47 4.2.1.47] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7H OCA].
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1N7H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N7H OCA].
==Reference==
==Reference==
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Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity., Mulichak AM, Bonin CP, Reiter WD, Garavito RM, Biochemistry. 2002 Dec 31;41(52):15578-89. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12501186 12501186]
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Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity., Mulichak AM, Bonin CP, Reiter WD, Garavito RM, Biochemistry. 2002 Dec 31;41(52):15578-89. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12501186 12501186]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: GDP-mannose 4,6-dehydratase]]
[[Category: GDP-mannose 4,6-dehydratase]]
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[[Category: short-chain dehydrogenase/reductase]]
[[Category: short-chain dehydrogenase/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:07 2008''

Revision as of 10:53, 20 March 2008


PDB ID 1n7h

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands: and
Gene: mur1 (Arabidopsis thaliana)
Activity: GDP-mannose 4,6-dehydratase, with EC number 4.2.1.47
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of GDP-mannose 4,6-dehydratase ternary complex with NADPH and GDP


Overview

GDP-D-mannose 4,6-dehydratase catalyzes the first step in the de novo synthesis of GDP-L-fucose, the activated form of L-fucose, which is a component of glycoconjugates in plants known to be important to the development and strength of stem tissues. We have determined the three-dimensional structure of the MUR1 dehydratase isoform from Arabidopsis thaliana complexed with its NADPH cofactor as well as with the ligands GDP and GDP-D-rhamnose. MUR1 is a member of the nucleoside-diphosphosugar modifying subclass of the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr, and Ser/Thr residues. MUR1 is the first member of this subfamily to be observed as a tetramer, the interface of which reveals a close and intimate overlap of neighboring NADP(+)-binding sites. The GDP moiety of the substrate also binds in an unusual syn conformation. The protein-ligand interactions around the hexose moiety of the substrate support the importance of the conserved triad residues and an additional Glu side chain serving as a general base for catalysis. Phe and Arg side chains close to the hexose ring may serve to confer substrate specificity at the O2 position. In the MUR1/GDP-D-rhamnose complex, a single unique monomer within the protein tetramer that has an unoccupied substrate site highlights the conformational changes that accompany substrate binding and may suggest the existence of negative cooperativity in MUR1 function.

About this Structure

1N7H is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Structure of the MUR1 GDP-mannose 4,6-dehydratase from Arabidopsis thaliana: implications for ligand binding and specificity., Mulichak AM, Bonin CP, Reiter WD, Garavito RM, Biochemistry. 2002 Dec 31;41(52):15578-89. PMID:12501186

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