2za2: Difference between revisions

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[[Image:2za2.~~jpg~~|left|200px]]

[[Image:2za2.png|left|200px]]

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~~'''~~Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum~~'''~~

===Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum===

~~==Overview==~~

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~~Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses~~ the ~~decarboxylation of orotidine 5'-monophosphate (OMP)~~ to ~~uridine 5'-monophosphate (UMP). Here, we report~~ the ~~X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum~~ (~~PfOMPDC)~~ at 2.~~7, 2~~.~~65 and 2.65 A~~, ~~respectively. The structural analysis provides~~ the ~~substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site~~. ~~The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure~~-~~based optimization of antimalarial drugs.~~

The line below this paragraph, {{ABSTRACT_PUBMED_17981823}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 17981823 is the PubMed ID number.

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==About this Structure==

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[[Category: Plasmodium falciparum]]

[[Category: Pyrimidine biosynthesis]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 20~~:05:13 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:52:51 2008''

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-[[Image:2za2.jpg|left|200px]]
+{{Seed}}
+[[Image:2za2.png|left|200px]]
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 {{STRUCTURE_2za2|  PDB=2za2  |  SCENE=  }}
-'''Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum'''
+===Crystal Structure of the apo-form of orotidine-5'-monophosphate decarboxylase from P.falciparum===
-==Overview==
+<!--
-Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 A, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.
+The line below this paragraph, {{ABSTRACT_PUBMED_17981823}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17981823 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17981823}}
 ==About this Structure==
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 [[Category: Plasmodium falciparum]]
 [[Category: Pyrimidine biosynthesis]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:05:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:52:51 2008''