1zn4

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{{Theoretical_model}}
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[[Image:1zn4.png|left|200px]]
 
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==NAD-DEPENDENT METHYLENETETRAHYDROFOLATE DEHYDROGENASE- CYCLOHYDROLASE WITH BOUND NAD AND PHOSPHATE==
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The line below this paragraph, containing "STRUCTURE_1zn4", creates the "Structure Box" on the page.
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<StructureSection load='1zn4' size='340' side='right'caption='[[1zn4]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZN4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zn4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1zn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zn4 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1zn4| PDB=1zn4 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial NAD-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase (NMDMC) is believed to have evolved from a trifunctional NADP-dependent methylenetetrahydrofolate dehydrogenase-cyclohydrolase-synthetase. It is unique in its absolute requirement for inorganic phosphate and magnesium ions to support dehydrogenase activity. To enable us to investigate the roles of these ions, a homology model of human NMDMC was constructed based on the structures of three homologous proteins. The model supports the hypothesis that the absolutely required Pi can bind in close proximity to the 2'-hydroxyl of NAD through interactions with Arg166 and Arg198. The characterization of mutants of Arg166, Asp190, and Arg198 show that Arg166 is primarily responsible for Pi binding, while Arg198 plays a secondary role, assisting in binding and properly orienting the ion in the cofactor binding site. Asp190 helps to properly position Arg166. Mutants of Asp133 suggest that the magnesium ion interacts with both Pi and the aspartate side chain and plays a role in positioning Pi and NAD. NMDMC uses Pi and magnesium to adapt an NADP binding site for NAD binding. This adaptation represents a novel variation of the classic Rossmann fold.
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===NAD-DEPENDENT METHYLENETETRAHYDROFOLATE DEHYDROGENASE- CYCLOHYDROLASE WITH BOUND NAD AND PHOSPHATE===
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Magnesium and phosphate ions enable NAD binding to methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase.,Christensen KE, Mirza IA, Berghuis AM, Mackenzie RE J Biol Chem. 2005 Oct 7;280(40):34316-23. Epub 2005 Aug 11. PMID:16100107<ref>PMID:16100107</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16100107}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1zn4" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16100107 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16100107}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZN4 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:16100107</ref><references group="xtra"/>
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[[Category: Berghuis, A M]]
[[Category: Berghuis, A M]]
[[Category: Christensen, K E]]
[[Category: Christensen, K E]]
[[Category: Mackenzie, R E]]
[[Category: Mackenzie, R E]]
[[Category: Mirza, I A]]
[[Category: Mirza, I A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 09:23:39 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

NAD-DEPENDENT METHYLENETETRAHYDROFOLATE DEHYDROGENASE- CYCLOHYDROLASE WITH BOUND NAD AND PHOSPHATE

PDB ID 1zn4

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OCA

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