1wva

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{{STRUCTURE_1wva| PDB=1wva | SCENE= }}
{{STRUCTURE_1wva| PDB=1wva | SCENE= }}
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'''Crystal structure of human arginase I from twinned crystal'''
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===Crystal structure of human arginase I from twinned crystal===
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==Overview==
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Human arginase I is a potential target for therapeutic intervention in diseases linked to compromised l-arginine homeostasis. Here, we report high-affinity binding of the reaction coordinate analogue inhibitors 2(S)-amino-6-boronohexanoic acid (ABH, Kd = 5 nM) and S-(2-boronoethyl)-l-cysteine (BEC, Kd = 270 nM) to human arginase I, and we report x-ray crystal structures of the respective enzyme-inhibitor complexes at 1.29- and 1.94-A resolution determined from crystals twinned by hemihedry. The ultrahigh-resolution structure of the human arginase I-ABH complex yields an unprecedented view of the binuclear manganese cluster and illuminates the structural basis for nanomolar affinity: bidentate inner-sphere boronate-manganese coordination interactions and fully saturated hydrogen bond networks with inhibitor alpha-amino and alpha-carboxylate groups. These interactions are therefore implicated in the stabilization of the transition state for l-arginine hydrolysis. Electron density maps also reveal that active-site residue H141 is protonated as the imidazolium cation. The location of H141 is such that it could function as a general acid to protonate the leaving amino group of l-ornithine during catalysis, and this is a revised mechanistic proposal for arginase. This work serves as a foundation for studying the structural and chemical biology of arginase I in the immune response, and we demonstrate the inhibition of arginase activity by ABH in human and murine myeloid cells.
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(as it appears on PubMed at http://www.pubmed.gov), where 16141327 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16141327}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16141327 16141327]
Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16141327 16141327]
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Human arginase II: crystal structure and physiological role in male and female sexual arousal., Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW, Biochemistry. 2003 Jul 22;42(28):8445-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12859189 12859189]
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Twinned crystal]]
[[Category: Twinned crystal]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:11:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:30:09 2008''

Revision as of 12:30, 27 July 2008

Image:1wva.png

Template:STRUCTURE 1wva

Crystal structure of human arginase I from twinned crystal

Template:ABSTRACT PUBMED 16141327

About this Structure

1WVA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response., Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW, Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. PMID:16141327

Human arginase II: crystal structure and physiological role in male and female sexual arousal., Cama E, Colleluori DM, Emig FA, Shin H, Kim SW, Kim NN, Traish AM, Ash DE, Christianson DW, Biochemistry. 2003 Jul 22;42(28):8445-51. PMID:12859189

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